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Contents |
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(+ 6 more)
271 a.a.
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(+ 6 more)
241 a.a.
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Rnase ph core of the archaeal exosome in complex with a5 RNA
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Structure:
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Probable exosome complex exonuclease 2. Chain: a, c, e, g, i, k, m, o, q, s, u, w. Engineered: yes. Probable exosome complex exonuclease 1. Chain: b, d, f, h, j, l, n, p, r, t, v, x. Engineered: yes
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Source:
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Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.10Å
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R-factor:
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0.276
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R-free:
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0.289
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Authors:
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E.Lorentzen,E.Conti
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Key ref:
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E.Lorentzen
and
E.Conti
(2005).
Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core.
Mol Cell,
20,
473-481.
PubMed id:
DOI:
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Date:
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04-Oct-05
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Release date:
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23-Nov-05
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X:
E.C.3.1.13.-
- ?????
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DOI no:
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Mol Cell
20:473-481
(2005)
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PubMed id:
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Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core.
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E.Lorentzen,
E.Conti.
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ABSTRACT
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The exosome is a macromolecular complex that plays fundamental roles in the
biogenesis and turnover of a large number of RNA species. Here we report the
crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus
exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft
recognizes four nucleotides in a sequence-unspecific manner, mainly by
electrostatic interactions with the phosphate groups. Interactions at the 2'
hydroxyls of the sugars provide specificity for RNA over DNA. The structures
show both the bound substrate and the cleaved product of the reaction,
suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the
exosome.
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Selected figure(s)
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Figure 1.
Figure 1. View of the S. solfataricus Rrp41-Rrp42 Exosome
Core Bound to a Short Single-Stranded RNA
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Figure 3.
Figure 3. Reaction Mechanism
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
20,
473-481)
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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C.C.Yang,
Y.T.Wang,
Y.Y.Hsiao,
L.G.Doudeva,
P.H.Kuo,
S.Y.Chow,
and
H.S.Yuan
(2010).
Structural and biochemical characterization of CRN-5 and Rrp46: an exosome component participating in apoptotic DNA degradation.
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RNA,
16,
1748-1759.
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PDB codes:
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C.L.Ng,
D.G.Waterman,
A.A.Antson,
and
M.Ortiz-Lombardía
(2010).
Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.
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Acta Crystallogr D Biol Crystallogr,
66,
522-528.
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PDB code:
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C.Lu,
F.Ding,
and
A.Ke
(2010).
Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.
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PLoS One,
5,
e8739.
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PDB code:
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H.Malet,
M.Topf,
D.K.Clare,
J.Ebert,
F.Bonneau,
J.Basquin,
K.Drazkowska,
R.Tomecki,
A.Dziembowski,
E.Conti,
H.R.Saibil,
and
E.Lorentzen
(2010).
RNA channelling by the eukaryotic exosome.
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EMBO Rep,
11,
936-942.
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J.S.Luz,
C.R.Ramos,
M.C.Santos,
P.P.Coltri,
F.L.Palhano,
D.Foguel,
N.I.Zanchin,
and
C.C.Oliveira
(2010).
Identification of archaeal proteins that affect the exosome function in vitro.
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BMC Biochem,
11,
22.
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K.P.Callahan,
and
J.S.Butler
(2010).
TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6.
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J Biol Chem,
285,
3540-3547.
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M.Zhou,
and
C.V.Robinson
(2010).
When proteomics meets structural biology.
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Trends Biochem Sci,
35,
522-529.
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R.Tomecki,
K.Drazkowska,
and
A.Dziembowski
(2010).
Mechanisms of RNA degradation by the eukaryotic exosome.
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Chembiochem,
11,
938-945.
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S.Hartung,
T.Niederberger,
M.Hartung,
A.Tresch,
and
K.P.Hopfner
(2010).
Quantitative analysis of processive RNA degradation by the archaeal RNA exosome.
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Nucleic Acids Res,
38,
5166-5176.
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PDB codes:
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A.C.Graham,
D.L.Kiss,
and
E.D.Andrulis
(2009).
Core exosome-independent roles for Rrp6 in cell cycle progression.
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Mol Biol Cell,
20,
2242-2253.
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D.Schaeffer,
B.Tsanova,
A.Barbas,
F.P.Reis,
E.G.Dastidar,
M.Sanchez-Rotunno,
C.M.Arraiano,
and
A.van Hoof
(2009).
The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities.
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Nat Struct Mol Biol,
16,
56-62.
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F.Bonneau,
J.Basquin,
J.Ebert,
E.Lorentzen,
and
E.Conti
(2009).
The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation.
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Cell,
139,
547-559.
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PDB code:
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S.Nurmohamed,
B.Vaidialingam,
A.J.Callaghan,
and
B.F.Luisi
(2009).
Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly.
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J Mol Biol,
389,
17-33.
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PDB codes:
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E.Lorentzen,
J.Basquin,
and
E.Conti
(2008).
Structural organization of the RNA-degrading exosome.
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Curr Opin Struct Biol,
18,
709-713.
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H.Ibrahim,
J.Wilusz,
and
C.J.Wilusz
(2008).
RNA recognition by 3'-to-5' exonucleases: the substrate perspective.
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Biochim Biophys Acta,
1779,
256-265.
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J.C.Greimann,
and
C.D.Lima
(2008).
Reconstitution of RNA exosomes from human and Saccharomyces cerevisiae cloning, expression, purification, and activity assays.
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Methods Enzymol,
448,
185-210.
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M.Schmid,
and
T.H.Jensen
(2008).
The exosome: a multipurpose RNA-decay machine.
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Trends Biochem Sci,
33,
501-510.
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M.V.Falaleeva,
H.V.Chetverina,
V.I.Ugarov,
E.A.Uzlova,
and
A.B.Chetverin
(2008).
Factors influencing RNA degradation by Thermus thermophilus polynucleotide phosphorylase.
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FEBS J,
275,
2214-2226.
|
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|
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M.V.Navarro,
C.C.Oliveira,
N.I.Zanchin,
and
B.G.Guimarães
(2008).
Insights into the mechanism of progressive RNA degradation by the archaeal exosome.
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J Biol Chem,
283,
14120-14131.
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PDB codes:
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V.Portnoy,
G.Palnizky,
S.Yehudai-Resheff,
F.Glaser,
and
G.Schuster
(2008).
Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.
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RNA,
14,
297-309.
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Z.Shi,
W.Z.Yang,
S.Lin-Chao,
K.F.Chak,
and
H.S.Yuan
(2008).
Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation.
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RNA,
14,
2361-2371.
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PDB codes:
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A.Dziembowski,
E.Lorentzen,
E.Conti,
and
B.Séraphin
(2007).
A single subunit, Dis3, is essentially responsible for yeast exosome core activity.
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Nat Struct Mol Biol,
14,
15-22.
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A.Oddone,
E.Lorentzen,
J.Basquin,
A.Gasch,
V.Rybin,
E.Conti,
and
M.Sattler
(2007).
Structural and biochemical characterization of the yeast exosome component Rrp40.
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EMBO Rep,
8,
63-69.
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PDB code:
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C.M.Arraiano,
J.Bamford,
H.Brüssow,
A.J.Carpousis,
V.Pelicic,
K.Pflüger,
P.Polard,
and
J.Vogel
(2007).
Recent advances in the expression, evolution, and dynamics of prokaryotic genomes.
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J Bacteriol,
189,
6093-6100.
|
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|
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|
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E.Lorentzen,
A.Dziembowski,
D.Lindner,
B.Seraphin,
and
E.Conti
(2007).
RNA channelling by the archaeal exosome.
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| |
EMBO Rep,
8,
470-476.
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PDB codes:
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E.Wahle
(2007).
Wrong PH for RNA degradation.
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Nat Struct Mol Biol,
14,
5-7.
|
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H.W.Wang,
J.Wang,
F.Ding,
K.Callahan,
M.A.Bratkowski,
J.S.Butler,
E.Nogales,
and
A.Ke
(2007).
Architecture of the yeast Rrp44 exosome complex suggests routes of RNA recruitment for 3' end processing.
|
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Proc Natl Acad Sci U S A,
104,
16844-16849.
|
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J.A.Stead,
J.L.Costello,
M.J.Livingstone,
and
P.Mitchell
(2007).
The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein.
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Nucleic Acids Res,
35,
5556-5567.
|
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J.A.Worrall,
and
B.F.Luisi
(2007).
Information available at cut rates: structure and mechanism of ribonucleases.
|
| |
Curr Opin Struct Biol,
17,
128-137.
|
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|
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|
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K.M.Reinisch,
and
S.L.Wolin
(2007).
Emerging themes in non-coding RNA quality control.
|
| |
Curr Opin Struct Biol,
17,
209-214.
|
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|
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K.Sasaki,
T.Ose,
N.Okamoto,
K.Maenaka,
T.Tanaka,
H.Masai,
M.Saito,
T.Shirai,
and
D.Kohda
(2007).
Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA.
|
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EMBO J,
26,
2584-2593.
|
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|
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S.Hartung,
and
K.P.Hopfner
(2007).
The exosome, plugged.
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| |
EMBO Rep,
8,
456-457.
|
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|
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S.Lin-Chao,
N.T.Chiou,
and
G.Schuster
(2007).
The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines.
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J Biomed Sci,
14,
523-532.
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S.Vanacova,
and
R.Stefl
(2007).
The exosome and RNA quality control in the nucleus.
|
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EMBO Rep,
8,
651-657.
|
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|
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A.C.Graham,
D.L.Kiss,
and
E.D.Andrulis
(2006).
Differential distribution of exosome subunits at the nuclear lamina and in cytoplasmic foci.
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Mol Biol Cell,
17,
1399-1409.
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E.Lorentzen,
and
E.Conti
(2006).
The exosome and the proteasome: nano-compartments for degradation.
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| |
Cell,
125,
651-654.
|
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H.A.Vincent,
and
M.P.Deutscher
(2006).
Substrate recognition and catalysis by the exoribonuclease RNase R.
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| |
J Biol Chem,
281,
29769-29775.
|
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J.Houseley,
J.LaCava,
and
D.Tollervey
(2006).
RNA-quality control by the exosome.
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Nat Rev Mol Cell Biol,
7,
529-539.
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K.Büttner,
K.Wenig,
and
K.P.Hopfner
(2006).
The exosome: a macromolecular cage for controlled RNA degradation.
|
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Mol Microbiol,
61,
1372-1379.
|
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P.Walter,
F.Klein,
E.Lorentzen,
A.Ilchmann,
G.Klug,
and
E.Evguenieva-Hackenberg
(2006).
Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus.
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Mol Microbiol,
62,
1076-1089.
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Q.Liu,
J.C.Greimann,
and
C.D.Lima
(2006).
Reconstitution, activities, and structure of the eukaryotic RNA exosome.
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Cell,
127,
1223-1237.
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PDB code:
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S.F.Midtgaard,
J.Assenholt,
A.T.Jonstrup,
L.B.Van,
T.H.Jensen,
and
D.E.Brodersen
(2006).
Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.
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Proc Natl Acad Sci U S A,
103,
11898-11903.
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PDB codes:
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V.Portnoy,
and
G.Schuster
(2006).
RNA polyadenylation and degradation in different Archaea; roles of the exosome and RNase R.
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Nucleic Acids Res,
34,
5923-5931.
|
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A.K.Eggleston
(2005).
Threaded for degradation.
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Nat Struct Mol Biol,
12,
1029.
|
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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.
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}
}
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