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PDBsum entry 1zbf
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* Residue conservation analysis
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Enzyme class:
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E.C.3.1.26.4
- ribonuclease H.
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Reaction:
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Endonucleolytic cleavage to 5'-phosphomonoester.
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DOI no:
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Cell
121:1005-1016
(2005)
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PubMed id:
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Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis.
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M.Nowotny,
S.A.Gaidamakov,
R.J.Crouch,
W.Yang.
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ABSTRACT
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RNase H belongs to a nucleotidyl-transferase superfamily, which includes
transposase, retroviral integrase, Holliday junction resolvase, and RISC
nuclease Argonaute. We report the crystal structures of RNase H complexed with
an RNA/DNA hybrid and a mechanism for substrate recognition and
two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form
RNA strand and the B form DNA strand. Structure comparisons lead us to predict
the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is
a general feature of the superfamily. In nucleases, the two metal ions are
asymmetrically coordinated and have distinct roles in activating the nucleophile
and stabilizing the transition state. In transposases, they are symmetrically
coordinated and exchange roles to alternately activate a water and a 3'-OH for
successive strand cleavage and transfer by a ping-pong mechanism.
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Selected figure(s)
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Figure 2.
Figure 2. Structure and Sequence Comparison of Bh, E. coli,
and HIV RNases H
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Figure 5.
Figure 5. The Active Site
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2005,
121,
1005-1016)
copyright 2005.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Lapkouski,
L.Tian,
J.T.Miller,
S.F.Le Grice,
and
W.Yang
(2013).
Complexes of HIV-1 RT, NNRTI and RNA/DNA hybrid reveal a structure compatible with RNA degradation.
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Nat Struct Mol Biol,
20,
230-236.
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PDB codes:
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H.M.Sasaki,
and
Y.Tomari
(2012).
The true core of RNA silencing revealed.
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Nat Struct Mol Biol,
19,
657-660.
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K.Nakanishi,
D.E.Weinberg,
D.P.Bartel,
and
D.J.Patel
(2012).
Structure of yeast Argonaute with guide RNA.
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Nature,
486,
368-374.
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PDB code:
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P.Cherepanov,
G.N.Maertens,
and
S.Hare
(2011).
Structural insights into the retroviral DNA integration apparatus.
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Curr Opin Struct Biol,
21,
249-256.
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W.Yang
(2011).
Nucleases: diversity of structure, function and mechanism.
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Q Rev Biophys,
44,
1.
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X.Zhang,
H.Zhao,
S.Gao,
W.C.Wang,
S.Katiyar-Agarwal,
H.D.Huang,
N.Raikhel,
and
H.Jin
(2011).
Arabidopsis Argonaute 2 Regulates Innate Immunity via miRNA393(∗)-Mediated Silencing of a Golgi-Localized SNARE Gene, MEMB12.
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Mol Cell,
42,
356-366.
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A.B.Hickman,
M.Chandler,
and
F.Dyda
(2010).
Integrating prokaryotes and eukaryotes: DNA transposases in light of structure.
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Crit Rev Biochem Mol Biol,
45,
50-69.
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A.Herschhorn,
and
A.Hizi
(2010).
Retroviral reverse transcriptases.
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Cell Mol Life Sci,
67,
2717-2747.
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A.Sabogal,
and
D.C.Rio
(2010).
A green fluorescent protein solubility screen in E. coli reveals domain boundaries of the GTP-binding domain in the P element transposase.
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Protein Sci,
19,
2210-2218.
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B.Elsässer,
and
G.Fels
(2010).
Atomistic details of the associative phosphodiester cleavage in human ribonuclease H.
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Phys Chem Chem Phys,
12,
11081-11088.
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C.Claeys Bouuaert,
and
R.Chalmers
(2010).
Transposition of the human Hsmar1 transposon: rate-limiting steps and the importance of the flanking TA dinucleotide in second strand cleavage.
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Nucleic Acids Res,
38,
190-202.
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C.Claeys Bouuaert,
and
R.M.Chalmers
(2010).
Gene therapy vectors: the prospects and potentials of the cut-and-paste transposons.
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Genetica,
138,
473-484.
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C.S.Adamson,
and
E.O.Freed
(2010).
Novel approaches to inhibiting HIV-1 replication.
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Antiviral Res,
85,
119-141.
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E.Kanaya,
T.Sakabe,
N.T.Nguyen,
S.Koikeda,
Y.Koga,
K.Takano,
and
S.Kanaya
(2010).
Cloning of the RNase H genes from a metagenomic DNA library: identification of a new type 1 RNase H without a typical active-site motif.
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J Appl Microbiol,
109,
974-983.
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H.A.Watkins,
and
E.N.Baker
(2010).
Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.
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J Bacteriol,
192,
2878-2886.
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PDB code:
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H.P.Su,
Y.Yan,
G.S.Prasad,
R.F.Smith,
C.L.Daniels,
P.D.Abeywickrema,
J.C.Reid,
H.M.Loughran,
M.Kornienko,
S.Sharma,
J.A.Grobler,
B.Xu,
V.Sardana,
T.J.Allison,
P.D.Williams,
P.L.Darke,
D.J.Hazuda,
and
S.Munshi
(2010).
Structural basis for the inhibition of RNase H activity of HIV-1 reverse transcriptase by RNase H active site-directed inhibitors.
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J Virol,
84,
7625-7633.
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PDB codes:
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H.Sípová,
H.Vaisocherová,
J.StÄ›pánek,
and
J.Homola
(2010).
A dual surface plasmon resonance assay for the determination of ribonuclease H activity.
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Biosens Bioelectron,
26,
1605-1611.
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I.A.Murray,
S.K.Stickel,
and
R.J.Roberts
(2010).
Sequence-specific cleavage of RNA by Type II restriction enzymes.
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Nucleic Acids Res,
38,
8257-8268.
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I.V.Nesmelova,
and
P.B.Hackett
(2010).
DDE transposases: Structural similarity and diversity.
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Adv Drug Deliv Rev,
62,
1187-1195.
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J.S.Parker
(2010).
How to slice: snapshots of Argonaute in action.
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Silence,
1,
3.
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L.Krishnan,
X.Li,
H.L.Naraharisetty,
S.Hare,
P.Cherepanov,
and
A.Engelman
(2010).
Structure-based modeling of the functional HIV-1 intasome and its inhibition.
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Proc Natl Acad Sci U S A,
107,
15910-15915.
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M.Egli,
and
P.S.Pallan
(2010).
Crystallographic studies of chemically modified nucleic acids: a backward glance.
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Chem Biodivers,
7,
60-89.
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M.Nadal,
P.J.Mas,
P.J.Mas,
A.G.Blanco,
C.Arnan,
M.Solà,
D.J.Hart,
and
M.Coll
(2010).
Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain.
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Proc Natl Acad Sci U S A,
107,
16078-16083.
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PDB codes:
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M.P.Rychlik,
H.Chon,
S.M.Cerritelli,
P.Klimek,
R.J.Crouch,
and
M.Nowotny
(2010).
Crystal structures of RNase H2 in complex with nucleic acid reveal the mechanism of RNA-DNA junction recognition and cleavage.
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Mol Cell,
40,
658-670.
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PDB codes:
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N.Jongruja,
D.J.You,
E.Kanaya,
Y.Koga,
K.Takano,
and
S.Kanaya
(2010).
The N-terminal hybrid binding domain of RNase HI from Thermotoga maritima is important for substrate binding and Mg2+-dependent activity.
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FEBS J,
277,
4474-4489.
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N.M.Shaban,
S.Harvey,
F.W.Perrino,
and
T.Hollis
(2010).
The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction.
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J Biol Chem,
285,
3617-3624.
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PDB code:
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P.Cherepanov
(2010).
Integrase illuminated.
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EMBO Rep,
11,
328.
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S.Hare,
A.M.Vos,
R.F.Clayton,
J.W.Thuring,
M.D.Cummings,
and
P.Cherepanov
(2010).
Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.
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Proc Natl Acad Sci U S A,
107,
20057-20062.
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PDB codes:
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S.Hare,
S.S.Gupta,
E.Valkov,
A.Engelman,
and
P.Cherepanov
(2010).
Retroviral intasome assembly and inhibition of DNA strand transfer.
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Nature,
464,
232-236.
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PDB codes:
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S.Kitamura,
K.Fujishima,
A.Sato,
D.Tsuchiya,
M.Tomita,
and
A.Kanai
(2010).
Characterization of RNase HII substrate recognition using RNase HII-argonaute chimaeric enzymes from Pyrococcus furiosus.
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Biochem J,
426,
337-344.
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S.Shukla,
C.S.Sumaria,
and
P.I.Pradeepkumar
(2010).
Exploring chemical modifications for siRNA therapeutics: a structural and functional outlook.
|
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ChemMedChem,
5,
328-349.
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V.Salvatore,
N.Potenza,
U.Papa,
V.Nobile,
and
A.Russo
(2010).
Bacterial expression of mouse argonaute 2 for functional and mutational studies.
|
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Int J Mol Sci,
11,
745-753.
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A.V.Kazantsev,
A.A.Krivenko,
and
N.R.Pace
(2009).
Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA.
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RNA,
15,
266-276.
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PDB code:
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A.V.Kilshtain,
and
A.Warshel
(2009).
On the origin of the catalytic power of carboxypeptidase A and other metalloenzymes.
|
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Proteins,
77,
536-550.
|
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B.Dalhus,
A.S.Arvai,
I.Rosnes,
Ã.˜.E.Olsen,
P.H.Backe,
I.Alseth,
H.Gao,
W.Cao,
J.A.Tainer,
and
M.Bjørås
(2009).
Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair.
|
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Nat Struct Mol Biol,
16,
138-143.
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PDB codes:
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D.M.Himmel,
K.A.Maegley,
T.A.Pauly,
J.D.Bauman,
K.Das,
C.Dharia,
A.D.Clark,
K.Ryan,
M.J.Hickey,
R.A.Love,
S.H.Hughes,
S.Bergqvist,
and
E.Arnold
(2009).
Structure of HIV-1 reverse transcriptase with the inhibitor beta-Thujaplicinol bound at the RNase H active site.
|
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Structure,
17,
1625-1635.
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PDB codes:
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E.Rosta,
H.L.Woodcock,
B.R.Brooks,
and
G.Hummer
(2009).
Artificial reaction coordinate "tunneling" in free-energy calculations: the catalytic reaction of RNase H.
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J Comput Chem,
30,
1634-1641.
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E.Valkov,
S.S.Gupta,
S.Hare,
A.Helander,
P.Roversi,
M.McClure,
and
P.Cherepanov
(2009).
Functional and structural characterization of the integrase from the prototype foamy virus.
|
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Nucleic Acids Res,
37,
243-255.
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PDB code:
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H.M.Roth,
I.Tessmer,
B.Van Houten,
and
C.Kisker
(2009).
Bax1 is a novel endonuclease: implications for archaeal nucleotide excision repair.
|
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J Biol Chem,
284,
32272-32278.
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J.Bischerour,
C.Lu,
D.B.Roth,
and
R.Chalmers
(2009).
Base flipping in V(D)J recombination: insights into the mechanism of hairpin formation, the 12/23 rule, and the coordination of double-strand breaks.
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Mol Cell Biol,
29,
5889-5899.
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J.J.Champoux,
and
S.J.Schultz
(2009).
Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription.
|
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FEBS J,
276,
1506-1516.
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K.A.Majorek,
and
J.M.Bujnicki
(2009).
Modeling of Escherichia coli Endonuclease V structure in complex with DNA.
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J Mol Model,
15,
173-182.
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K.R.Simonetta,
S.L.Kazmirski,
E.R.Goedken,
A.J.Cantor,
B.A.Kelch,
R.McNally,
S.N.Seyedin,
D.L.Makino,
M.O'Donnell,
and
J.Kuriyan
(2009).
The mechanism of ATP-dependent primer-template recognition by a clamp loader complex.
|
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Cell,
137,
659-671.
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PDB codes:
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K.Ratcliff,
J.Corn,
and
S.Marqusee
(2009).
Structure, stability, and folding of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues.
|
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Biochemistry,
48,
5890-5898.
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PDB code:
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M.C.Siomi
(2009).
Short interfering RNA-mediated gene silencing; towards successful application in human patients.
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Adv Drug Deliv Rev,
61,
668-671.
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M.Jaskolski,
J.N.Alexandratos,
G.Bujacz,
and
A.Wlodawer
(2009).
Piecing together the structure of retroviral integrase, an important target in AIDS therapy.
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FEBS J,
276,
2926-2946.
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M.Jinek,
and
J.A.Doudna
(2009).
A three-dimensional view of the molecular machinery of RNA interference.
|
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Nature,
457,
405-412.
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M.L.Barreca,
N.Iraci,
L.De Luca,
and
A.Chimirri
(2009).
Induced-fit docking approach provides insight into the binding mode and mechanism of action of HIV-1 integrase inhibitors.
|
| |
ChemMedChem,
4,
1446-1456.
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M.Nowotny
(2009).
Retroviral integrase superfamily: the structural perspective.
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| |
EMBO Rep,
10,
144-151.
|
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|
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M.Nowotny,
and
W.Yang
(2009).
Structural and functional modules in RNA interference.
|
| |
Curr Opin Struct Biol,
19,
286-293.
|
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|
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S.G.Sarafianos,
B.Marchand,
K.Das,
D.M.Himmel,
M.A.Parniak,
S.H.Hughes,
and
E.Arnold
(2009).
Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition.
|
| |
J Mol Biol,
385,
693-713.
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S.M.Cerritelli,
and
R.J.Crouch
(2009).
Ribonuclease H: the enzymes in eukaryotes.
|
| |
FEBS J,
276,
1494-1505.
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T.Tadokoro,
and
S.Kanaya
(2009).
Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.
|
| |
FEBS J,
276,
1482-1493.
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V.Alvarado,
and
H.B.Scholthof
(2009).
Plant responses against invasive nucleic acids: RNA silencing and its suppression by plant viral pathogens.
|
| |
Semin Cell Dev Biol,
20,
1032-1040.
|
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Y.Wang,
S.Juranek,
H.Li,
G.Sheng,
G.S.Wardle,
T.Tuschl,
and
D.J.Patel
(2009).
Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes.
|
| |
Nature,
461,
754-761.
|
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PDB codes:
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A.C.Déclais,
and
D.M.Lilley
(2008).
New insight into the recognition of branched DNA structure by junction-resolving enzymes.
|
| |
Curr Opin Struct Biol,
18,
86-95.
|
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|
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C.Dash,
B.J.Scarth,
C.Badorrek,
M.Götte,
and
S.F.Le Grice
(2008).
Examining the ribonuclease H primer grip of HIV-1 reverse transcriptase by charge neutralization of RNA/DNA hybrids.
|
| |
Nucleic Acids Res,
36,
6363-6371.
|
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C.M.Dupureur
(2008).
Roles of metal ions in nucleases.
|
| |
Curr Opin Chem Biol,
12,
250-255.
|
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D.B.Ritchie,
M.J.Schellenberg,
E.M.Gesner,
S.A.Raithatha,
D.T.Stuart,
and
A.M.Macmillan
(2008).
Structural elucidation of a PRP8 core domain from the heart of the spliceosome.
|
| |
Nat Struct Mol Biol,
15,
1199-1205.
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PDB code:
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E.A.Abbondanzieri,
G.Bokinsky,
J.W.Rausch,
J.X.Zhang,
S.F.Le Grice,
and
X.Zhuang
(2008).
Dynamic binding orientations direct activity of HIV reverse transcriptase.
|
| |
Nature,
453,
184-189.
|
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H.A.Watkins,
and
E.N.Baker
(2008).
Cloning, expression, purification and preliminary crystallographic analysis of the RNase HI domain of the Mycobacterium tuberculosis protein Rv2228c as a maltose-binding protein fusion.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
746-749.
|
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H.Vaucheret
(2008).
Plant ARGONAUTES.
|
| |
Trends Plant Sci,
13,
350-358.
|
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J.Salon,
J.Jiang,
J.Sheng,
O.O.Gerlits,
and
Z.Huang
(2008).
Derivatization of DNAs with selenium at 6-position of guanine for function and crystal structure studies.
|
| |
Nucleic Acids Res,
36,
7009-7018.
|
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K.Syson,
C.Tomlinson,
B.R.Chapados,
J.R.Sayers,
J.A.Tainer,
N.H.Williams,
and
J.A.Grasby
(2008).
Three metal ions participate in the reaction catalyzed by t5 flap endonuclease.
|
| |
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Genome-wide identification, organization and phylogenetic analysis of Dicer-like, Argonaute and RNA-dependent RNA Polymerase gene families and their expression analysis during reproductive development and stress in rice.
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BMC Genomics,
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TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism.
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Nucleic Acids Res,
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Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.
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EMBO J,
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PDB code:
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N.Minakawa,
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Chembiochem,
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R.Mitra,
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piggyBac can bypass DNA synthesis during cut and paste transposition.
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EMBO J,
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Virus Res,
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S.Sun,
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The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces.
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Cell,
135,
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PDB codes:
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U.D.Priyakumar,
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Atomic detail investigation of the structure and dynamics of DNA.RNA hybrids: a molecular dynamics study.
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Structure and function of an RNase H domain at the heart of the spliceosome.
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EMBO J,
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PDB codes:
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W.Yang
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Nat Struct Mol Biol,
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Structure of the guide-strand-containing argonaute silencing complex.
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Nature,
456,
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PDB codes:
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Y.Wang,
S.Juranek,
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T.Tuschl,
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Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex.
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Nature,
456,
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PDB code:
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Z.J.Lu,
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Fundamental differences in the equilibrium considerations for siRNA and antisense oligodeoxynucleotide design.
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Nucleic Acids Res,
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J Mol Biol,
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PDB code:
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E.Karakas,
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Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.
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EMBO J,
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PDB codes:
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H.Kochiwa,
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Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes.
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BMC Evol Biol,
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BMC Bioinformatics,
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High resolution footprinting of the hepatitis C virus polymerase NS5B in complex with RNA.
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J Biol Chem,
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Conversion of pre-RISC to holo-RISC by Ago2 during assembly of RNAi complexes.
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RNA,
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Crystallization and preliminary X-ray analysis of Escherichia coli RNase HI-dsRNA complexes.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
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Insights from crystallographic studies into the structural and pairing properties of nucleic acid analogs and chemically modified DNA and RNA oligonucleotides.
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Annu Rev Biophys Biomol Struct,
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Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription.
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Mol Cell,
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PDB codes:
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N.H.Tolia,
and
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Slicer and the argonautes.
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Nat Chem Biol,
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Identification of the gene encoding a type 1 RNase H with an N-terminal double-stranded RNA binding domain from a psychrotrophic bacterium.
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FEBS J,
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Bacterial RNase P: a new view of an ancient enzyme.
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Nat Rev Microbiol,
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Examining Ty3 polypurine tract structure and function by nucleoside analog interference.
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J Biol Chem,
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Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex.
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Nature,
443,
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PDB codes:
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D.J.Patel,
J.B.Ma,
Y.R.Yuan,
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Y.Pei,
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Structural biology of RNA silencing and its functional implications.
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Cold Spring Harb Symp Quant Biol,
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D.J.You,
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Crystallization and preliminary crystallographic analysis of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
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D.Lim,
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Crystal structure of the moloney murine leukemia virus RNase H domain.
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J Virol,
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PDB code:
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D.Wang,
D.A.Bushnell,
K.D.Westover,
C.D.Kaplan,
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Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis.
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Cell,
127,
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PDB codes:
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F.Li,
S.Sarkhel,
C.J.Wilds,
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T.P.Prakash,
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2'-Fluoroarabino- and arabinonucleic acid show different conformations, resulting in deviating RNA affinities and processing of their heteroduplexes with RNA by RNase H.
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Biochemistry,
45,
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PDB codes:
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F.Renzi,
E.Caffarelli,
P.Laneve,
I.Bozzoni,
M.Brunori,
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The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.
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Proc Natl Acad Sci U S A,
103,
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PDB code:
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H.Chon,
T.Tadokoro,
N.Ohtani,
Y.Koga,
K.Takano,
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Identification of RNase HII from psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H.
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FEBS J,
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I.J.Macrae,
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A.Repic,
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Structural basis for double-stranded RNA processing by Dicer.
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Science,
311,
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PDB code:
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J.Gan,
J.E.Tropea,
B.P.Austin,
D.L.Court,
D.S.Waugh,
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Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III.
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Cell,
124,
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PDB code:
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J.M.Richardson,
A.Dawson,
N.O'Hagan,
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D.J.Finnegan,
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Mechanism of Mos1 transposition: insights from structural analysis.
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EMBO J,
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PDB code:
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J.R.Horton,
X.Zhang,
R.Maunus,
Z.Yang,
G.G.Wilson,
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DNA nicking by HinP1I endonuclease: bending, base flipping and minor groove expansion.
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Nucleic Acids Res,
34,
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PDB codes:
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J.S.Parker,
and
D.Barford
(2006).
Argonaute: A scaffold for the function of short regulatory RNAs.
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Trends Biochem Sci,
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J.S.Parker,
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Molecular mechanism of target RNA transcript recognition by Argonaute-guide complexes.
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Cold Spring Harb Symp Quant Biol,
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K.Moelling,
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Relationship between retroviral replication and RNA interference machineries.
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Cold Spring Harb Symp Quant Biol,
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L.Joshua-Tor
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The Argonautes.
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Cold Spring Harb Symp Quant Biol,
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L.Ponchon,
P.Boulanger,
G.Labesse,
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The endonuclease domain of bacteriophage terminases belongs to the resolvase/integrase/ribonuclease H superfamily: a bioinformatics analysis validated by a functional study on bacteriophage T5.
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J Biol Chem,
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M.Nowotny,
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Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release.
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EMBO J,
25,
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PDB codes:
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N.Potenza,
V.Salvatore,
A.Migliozzi,
V.Martone,
V.Nobile,
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Hybridase activity of human ribonuclease-1 revealed by a real-time fluorometric assay.
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Nucleic Acids Res,
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M.Maiti,
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The chemical nature of the 2'-substituent in the pentose-sugar dictates the pseudoaromatic character of the nucleobase (pKa) in DNA/RNA.
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Org Biomol Chem,
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S.J.Schultz,
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Sequence, distance, and accessibility are determinants of 5'-end-directed cleavages by retroviral RNases H.
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J Biol Chem,
281,
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S.Ricagno,
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Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family.
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Proc Natl Acad Sci U S A,
103,
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PDB code:
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T.L.Diamond,
and
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Role of metal ions in catalysis by HIV integrase analyzed using a quantitative PCR disintegration assay.
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Nucleic Acids Res,
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Mg2+ dependency of HIV-1 reverse transcription, inhibition by nucleoside analogues and resistance.
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Nucleic Acids Res,
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W.Yang,
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Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity.
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Mol Cell,
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Structural basis for non-catalytic and catalytic activities of ribonuclease III.
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Acta Crystallogr D Biol Crystallogr,
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Isolation of a site-specifically modified RNA from an unmodified transcript.
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Nucleic Acids Res,
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Y.Zuo,
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Structural basis for processivity and single-strand specificity of RNase II.
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Mol Cell,
24,
149-156.
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PDB code:
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D.G.Vassylyev,
V.Svetlov,
M.N.Vassylyeva,
A.Perederina,
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Structural basis for transcription inhibition by tagetitoxin.
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Nat Struct Mol Biol,
12,
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PDB code:
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J.Y.Lee,
J.Chang,
N.Joseph,
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D.N.Rao,
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MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage.
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Mol Cell,
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PDB codes:
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K.D.Robertson
(2005).
DNA methylation and human disease.
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Nat Rev Genet,
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T.M.Hall
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Structure and function of argonaute proteins.
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Structure,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
|
Links
