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PDBsum entry 1fuk
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.6.4.13
- Rna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
97:13080-13085
(2000)
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PubMed id:
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Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.
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J.M.Caruthers,
E.R.Johnson,
D.B.McKay.
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ABSTRACT
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The eukaryotic translation initiation factor 4A (eIF4A) is a member of the
DEA(D/H)-box RNA helicase family, a diverse group of proteins that couples an
ATPase activity to RNA binding and unwinding. Previous work has provided the
structure of the amino-terminal, ATP-binding domain of eIF4A. Extending those
results, we have solved the structure of the carboxyl-terminal domain of eIF4A
with data to 1.75 A resolution; it has a parallel alpha-beta topology that
superimposes, with minor variations, on the structures and conserved motifs of
the equivalent domain in other, distantly related helicases. Using data to 2.8 A
resolution and molecular replacement with the refined model of the
carboxyl-terminal domain, we have completed the structure of full-length eIF4A;
it is a "dumbbell" structure consisting of two compact domains
connected by an extended linker. By using the structures of other helicases as a
template, compact structures can be modeled for eIF4A that suggest (i) helicase
motif IV binds RNA; (ii) Arg-298, which is conserved in the DEA(D/H)-box RNA
helicase family but is absent from many other helicases, also binds RNA; and
(iii) motifs V and VI "link" the carboxyl-terminal domain to the
amino-terminal domain through interactions with ATP and the DEA(D/H) motif,
providing a mechanism for coupling ATP binding and hydrolysis with
conformational changes that modulate RNA binding.
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Selected figure(s)
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Figure 1.
Fig. 1. Structure of the carboxyl-terminal domain of
eIF4A. (A) Stereoview, ribbon drawing of the structure.
Conserved motifs are colored as follows: motif IV, VIFCNTRR,
residues 263-270, green; "conserved R" motif, residue Arg-298,
purple; motif V, RGID, residues 321-324, magenta; motif VI,
HRIGRGGR, residues 345-352, cyan. The strands of the  -sheet are
labeled sequentially. This and subsequent ribbon drawings were
prepared with MOLSCRIPT (34) and rendered with RASTER3D (35).
(B) Topology diagram of the structure. -Strands are
shown as arrows;  -helices,
as cylinders. -Strands and
-helices
are labeled sequentially as 1-7 and [1]- [6],
respectively. Sequences of the conserved motifs are shown in
boxes; residues whose side chains are illustrated in A and
subsequent figures are underlined.
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Figure 2.
Fig. 2. Ribbon drawing of the structure of full-length
eIF4A. The amino- and carboxyl-terminal domains are colored
silver and gold, respectively; the 11-residue linker connecting
them is colored black. The conserved amino-terminal motifs are
colored as follows: motif I, Walker A motif ASQSGTGKT, residues
65-72, blue; motif Ia, PTRELA, residues 97-102, yellow; GG,
residues 125-126, orange; TPGR, residues 145-148, pink; motif
II, Walker B motif DEAD, residues 169-172, red; motif III, SAT,
residues 200-202, green. The conserved carboxyl-terminal motifs
are colored as described in Fig. 1A.
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Figures were
selected
by the author.
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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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F.Mueller-Planitz,
H.Klinker,
J.Ludwigsen,
and
P.B.Becker
(2013).
The ATPase domain of ISWI is an autonomous nucleosome remodeling machine.
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Nat Struct Mol Biol,
20,
82-89.
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A.Parsyan,
Y.Svitkin,
D.Shahbazian,
C.Gkogkas,
P.Lasko,
W.C.Merrick,
and
N.Sonenberg
(2011).
mRNA helicases: the tacticians of translational control.
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Nat Rev Mol Cell Biol,
12,
235-245.
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B.Kolaczkowski,
D.N.Hupalo,
and
A.D.Kern
(2011).
Recurrent adaptation in RNA interference genes across the Drosophila phylogeny.
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Mol Biol Evol,
28,
1033-1042.
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J.Strohmeier,
I.Hertel,
U.Diederichsen,
M.G.Rudolph,
and
D.Klostermeier
(2011).
Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop.
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Biol Chem,
392,
357-369.
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PDB codes:
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M.Hilbert,
F.Kebbel,
A.Gubaev,
and
D.Klostermeier
(2011).
eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism.
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Nucleic Acids Res,
39,
2260-2270.
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P.Linder,
and
E.Jankowsky
(2011).
From unwinding to clamping - the DEAD box RNA helicase family.
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Nat Rev Mol Cell Biol,
12,
505-516.
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E.R.Yassin,
A.M.Abdul-Nabi,
A.Takeda,
and
N.R.Yaseen
(2010).
Effects of the NUP98-DDX10 oncogene on primary human CD34+ cells: role of a conserved helicase motif.
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Leukemia,
24,
1001-1011.
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Y.He,
G.R.Andersen,
and
K.H.Nielsen
(2010).
Structural basis for the function of DEAH helicases.
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EMBO Rep,
11,
180-186.
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PDB code:
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A.Marintchev,
K.A.Edmonds,
B.Marintcheva,
E.Hendrickson,
M.Oberer,
C.Suzuki,
B.Herdy,
N.Sonenberg,
and
G.Wagner
(2009).
Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation.
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Cell,
136,
447-460.
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D.Klostermeier,
and
M.G.Rudolph
(2009).
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
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Nucleic Acids Res,
37,
421-430.
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PDB codes:
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F.Tritschler,
J.E.Braun,
A.Eulalio,
V.Truffault,
E.Izaurralde,
and
O.Weichenrieder
(2009).
Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B.
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Mol Cell,
33,
661-668.
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PDB codes:
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J.H.Chang,
Y.H.Cho,
S.Y.Sohn,
J.M.Choi,
A.Kim,
Y.C.Kim,
S.K.Jang,
and
Y.Cho
(2009).
Crystal structure of the eIF4A-PDCD4 complex.
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Proc Natl Acad Sci U S A,
106,
3148-3153.
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PDB code:
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J.M.Tsay,
J.Sippy,
M.Feiss,
and
D.E.Smith
(2009).
The Q motif of a viral packaging motor governs its force generation and communicates ATP recognition to DNA interaction.
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Proc Natl Acad Sci U S A,
106,
14355-14360.
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J.Napetschnig,
S.A.Kassube,
E.W.Debler,
R.W.Wong,
G.Blobel,
and
A.Hoelz
(2009).
Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19.
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Proc Natl Acad Sci U S A,
106,
3089-3094.
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PDB codes:
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L.Zhang,
T.Xu,
C.Maeder,
L.O.Bud,
J.Shanks,
J.Nix,
C.Guthrie,
J.A.Pleiss,
and
R.Zhao
(2009).
Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2.
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Nat Struct Mol Biol,
16,
731-739.
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PDB code:
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M.E.Budiman,
J.L.Bubenik,
A.C.Miniard,
L.M.Middleton,
C.A.Gerber,
A.Cash,
and
D.M.Driscoll
(2009).
Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation.
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Mol Cell,
35,
479-489.
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M.G.Rudolph,
and
D.Klostermeier
(2009).
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.
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RNA,
15,
1993-2001.
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PDB codes:
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M.G.Rudolph,
J.G.Wittmann,
and
D.Klostermeier
(2009).
Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
248-252.
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M.Hilbert,
A.R.Karow,
and
D.Klostermeier
(2009).
The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.
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Biol Chem,
390,
1237-1250.
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P.G.Loh,
H.S.Yang,
M.A.Walsh,
Q.Wang,
X.Wang,
Z.Cheng,
D.Liu,
and
H.Song
(2009).
Structural basis for translational inhibition by the tumour suppressor Pdcd4.
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EMBO J,
28,
274-285.
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PDB codes:
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S.Chimnaronk,
T.Suzuki,
T.Manita,
Y.Ikeuchi,
M.Yao,
T.Suzuki,
and
I.Tanaka
(2009).
RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon.
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EMBO J,
28,
1362-1373.
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PDB code:
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S.H.Ling,
Z.Cheng,
and
H.Song
(2009).
Structural aspects of RNA helicases in eukaryotic mRNA decay.
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Biosci Rep,
29,
339-349.
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Y.Fujita,
M.Oe,
T.Tutsumino,
S.Morino,
H.Imataka,
K.Tomoo,
and
T.Ishida
(2009).
Domain-dependent interaction of eukaryotic initiation factor eIF4A for binding to middle and C-terminal domains of eIF4G.
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J Biochem,
146,
359-368.
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Z.Y.Dossani,
C.S.Weirich,
J.P.Erzberger,
J.M.Berger,
and
K.Weis
(2009).
Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
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Proc Natl Acad Sci U S A,
106,
16251-16256.
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PDB code:
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A.Obarska-Kosinska,
J.E.Taylor,
P.Callow,
J.Orlowski,
J.M.Bujnicki,
and
G.G.Kneale
(2008).
HsdR subunit of the type I restriction-modification enzyme EcoR124I: biophysical characterisation and structural modelling.
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J Mol Biol,
376,
438-452.
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B.Theissen,
A.R.Karow,
J.Köhler,
A.Gubaev,
and
D.Klostermeier
(2008).
Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase.
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Proc Natl Acad Sci U S A,
105,
548-553.
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E.J.Enemark,
and
L.Joshua-Tor
(2008).
On helicases and other motor proteins.
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Curr Opin Struct Biol,
18,
243-257.
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H.Le Hir,
and
G.R.Andersen
(2008).
Structural insights into the exon junction complex.
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Curr Opin Struct Biol,
18,
112-119.
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J.Banroques,
O.Cordin,
M.Doère,
P.Linder,
and
N.K.Tanner
(2008).
A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins.
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Mol Cell Biol,
28,
3359-3371.
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K.Manikandan,
D.Pal,
S.Ramakumar,
N.E.Brener,
S.S.Iyengar,
and
G.Seetharaman
(2008).
Functionally important segments in proteins dissected using Gene Ontology and geometric clustering of peptide fragments.
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Genome Biol,
9,
R52.
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L.M.Elles,
and
O.C.Uhlenbeck
(2008).
Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype.
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Nucleic Acids Res,
36,
41-50.
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P.Schütz,
M.Bumann,
A.E.Oberholzer,
C.Bieniossek,
H.Trachsel,
M.Altmann,
and
U.Baumann
(2008).
Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.
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Proc Natl Acad Sci U S A,
105,
9564-9569.
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PDB codes:
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S.Wang,
M.T.Overgaard,
Y.Hu,
and
D.B.McKay
(2008).
The Bacillus subtilis RNA helicase YxiN is distended in solution.
|
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Biophys J,
94,
L01-L03.
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X.Zhang,
T.Nakashima,
Y.Kakuta,
M.Yao,
I.Tanaka,
and
M.Kimura
(2008).
Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3.
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Protein Sci,
17,
136-145.
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PDB code:
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A.R.Karow,
B.Theissen,
and
D.Klostermeier
(2007).
Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains.
|
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FEBS J,
274,
463-473.
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B.Rodamilans,
and
G.Montoya
(2007).
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
283-286.
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PDB code:
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E.Jankowsky,
and
M.E.Fairman
(2007).
RNA helicases--one fold for many functions.
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Curr Opin Struct Biol,
17,
316-324.
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F.Bleichert,
and
S.J.Baserga
(2007).
The long unwinding road of RNA helicases.
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Mol Cell,
27,
339-352.
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K.A.Satyshur,
G.A.Worzalla,
L.S.Meyer,
E.K.Heiniger,
K.G.Aukema,
A.M.Misic,
and
K.T.Forest
(2007).
Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.
|
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Structure,
15,
363-376.
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PDB codes:
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M.R.Singleton,
M.S.Dillingham,
and
D.B.Wigley
(2007).
Structure and mechanism of helicases and nucleic acid translocases.
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Annu Rev Biochem,
76,
23-50.
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M.Valencia-Burton,
R.M.McCullough,
C.R.Cantor,
and
N.E.Broude
(2007).
RNA visualization in live bacterial cells using fluorescent protein complementation.
|
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Nat Methods,
4,
421-427.
|
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R.Tuteja
(2007).
Helicases - feasible antimalarial drug target for Plasmodium falciparum.
|
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FEBS J,
274,
4699-4704.
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S.Watanabe,
K.Y.Tomizaki,
T.Takahashi,
K.Usui,
K.Kajikawa,
and
H.Mihara
(2007).
Interactions between peptides containing nucleobase amino acids and T7 phages displaying S. cerevisiae proteins.
|
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Biopolymers,
88,
131-140.
|
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W.K.Low,
Y.Dang,
S.Bhat,
D.Romo,
and
J.O.Liu
(2007).
Substrate-dependent targeting of eukaryotic translation initiation factor 4A by pateamine A: negation of domain-linker regulation of activity.
|
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Chem Biol,
14,
715-727.
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D.Keramisanou,
N.Biris,
I.Gelis,
G.Sianidis,
S.Karamanou,
A.Economou,
and
C.G.Kalodimos
(2006).
Disorder-order folding transitions underlie catalysis in the helicase motor of SecA.
|
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Nat Struct Mol Biol,
13,
594-602.
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J.M.Caruthers,
Y.Hu,
and
D.B.McKay
(2006).
Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
1191-1195.
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PDB code:
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L.Fan,
A.S.Arvai,
P.K.Cooper,
S.Iwai,
F.Hanaoka,
and
J.A.Tainer
(2006).
Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair.
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Mol Cell,
22,
27-37.
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PDB codes:
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M.Barhoumi,
N.K.Tanner,
J.Banroques,
P.Linder,
and
I.Guizani
(2006).
Leishmania infantum LeIF protein is an ATP-dependent RNA helicase and an eIF4A-like factor that inhibits translation in yeast.
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FEBS J,
273,
5086-5100.
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R.Dhalia,
N.Marinsek,
C.R.Reis,
R.Katz,
J.R.Muniz,
N.Standart,
M.Carrington,
and
O.P.de Melo Neto
(2006).
The two eIF4A helicases in Trypanosoma brucei are functionally distinct.
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Nucleic Acids Res,
34,
2495-2507.
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S.Wang,
Y.Hu,
M.T.Overgaard,
F.V.Karginov,
O.C.Uhlenbeck,
and
D.B.McKay
(2006).
The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold.
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RNA,
12,
959-967.
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PDB code:
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T.Matsui,
K.Hogetsu,
J.Usukura,
T.Sato,
T.Kumasaka,
Y.Akao,
and
N.Tanaka
(2006).
Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes.
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Genes Cells,
11,
439-452.
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PDB code:
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T.Sengoku,
O.Nureki,
A.Nakamura,
S.Kobayashi,
and
S.Yokoyama
(2006).
Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa.
|
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Cell,
125,
287-300.
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PDB code:
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T.Shibuya,
T.Ã.˜.Tange,
M.E.Stroupe,
and
M.J.Moore
(2006).
Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay.
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RNA,
12,
360-374.
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H.Zakowicz,
H.S.Yang,
C.Stark,
A.Wlodawer,
N.Laronde-Leblanc,
and
N.H.Colburn
(2005).
Mutational analysis of the DEAD-box RNA helicase eIF4AII characterizes its interaction with transformation suppressor Pdcd4 and eIF4GI.
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| |
RNA,
11,
261-274.
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J.Wu,
A.K.Bera,
R.J.Kuhn,
and
J.L.Smith
(2005).
Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing.
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| |
J Virol,
79,
10268-10277.
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PDB codes:
|
|
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|
|
L.Ballut,
B.Marchadier,
A.Baguet,
C.Tomasetto,
B.Séraphin,
and
H.Le Hir
(2005).
The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity.
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Nat Struct Mol Biol,
12,
861-869.
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M.C.Zittel,
and
J.L.Keck
(2005).
Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: role of a highly conserved aromatic-rich sequence.
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Nucleic Acids Res,
33,
6982-6991.
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M.E.Bordeleau,
J.Matthews,
J.M.Wojnar,
L.Lindqvist,
O.Novac,
E.Jankowsky,
N.Sonenberg,
P.Northcote,
P.Teesdale-Spittle,
and
J.Pelletier
(2005).
Stimulation of mammalian translation initiation factor eIF4A activity by a small molecule inhibitor of eukaryotic translation.
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Proc Natl Acad Sci U S A,
102,
10460-10465.
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M.Oberer,
A.Marintchev,
and
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(2005).
Structural basis for the enhancement of eIF4A helicase activity by eIF4G.
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| |
Genes Dev,
19,
2212-2223.
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N.H.Thomä,
B.K.Czyzewski,
A.A.Alexeev,
A.V.Mazin,
S.C.Kowalczykowski,
and
N.P.Pavletich
(2005).
Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54.
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| |
Nat Struct Mol Biol,
12,
350-356.
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|
PDB code:
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|
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|
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|
|
T.Sakamoto,
A.Oguro,
G.Kawai,
T.Ohtsu,
and
Y.Nakamura
(2005).
NMR structures of double loops of an RNA aptamer against mammalian initiation factor 4A.
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| |
Nucleic Acids Res,
33,
745-754.
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PDB codes:
|
|
|
|
|
|
|
|
W.K.Low,
Y.Dang,
T.Schneider-Poetsch,
Z.Shi,
N.S.Choi,
W.C.Merrick,
D.Romo,
and
J.O.Liu
(2005).
Inhibition of eukaryotic translation initiation by the marine natural product pateamine A.
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| |
Mol Cell,
20,
709-722.
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Z.Cheng,
J.Coller,
R.Parker,
and
H.Song
(2005).
Crystal structure and functional analysis of DEAD-box protein Dhh1p.
|
| |
RNA,
11,
1258-1270.
|
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|
PDB code:
|
|
|
|
|
|
|
|
A.B.Carmel,
and
B.W.Matthews
(2004).
Crystal structure of the BstDEAD N-terminal domain: a novel DEAD protein from Bacillus stearothermophilus.
|
| |
RNA,
10,
66-74.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
D.J.Fitzgerald,
C.DeLuca,
I.Berger,
H.Gaillard,
R.Sigrist,
K.Schimmele,
and
T.J.Richmond
(2004).
Reaction cycle of the yeast Isw2 chromatin remodeling complex.
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| |
EMBO J,
23,
3836-3843.
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E.A.Sickmier,
K.N.Kreuzer,
and
S.W.White
(2004).
The crystal structure of the UvsW helicase from bacteriophage T4.
|
| |
Structure,
12,
583-592.
|
|
|
PDB code:
|
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|
|
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|
|
H.S.Yang,
M.H.Cho,
H.Zakowicz,
G.Hegamyer,
N.Sonenberg,
and
N.H.Colburn
(2004).
A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A.
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| |
Mol Cell Biol,
24,
3894-3906.
|
|
|
|
|
|
|
H.Shi,
O.Cordin,
C.M.Minder,
P.Linder,
and
R.M.Xu
(2004).
Crystal structure of the human ATP-dependent splicing and export factor UAP56.
|
| |
Proc Natl Acad Sci U S A,
101,
17628-17633.
|
|
|
PDB codes:
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|
|
J.Kawaoka,
E.Jankowsky,
and
A.M.Pyle
(2004).
Backbone tracking by the SF2 helicase NPH-II.
|
| |
Nat Struct Mol Biol,
11,
526-530.
|
|
|
|
|
|
|
K.L.Sim,
and
T.P.Creamer
(2004).
Protein simple sequence conservation.
|
| |
Proteins,
54,
629-638.
|
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|
|
|
|
L.D.Kapp,
and
J.R.Lorsch
(2004).
The molecular mechanics of eukaryotic translation.
|
| |
Annu Rev Biochem,
73,
657-704.
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|
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|
|
M.Abdelhaleem
(2004).
Do human RNA helicases have a role in cancer?
|
| |
Biochim Biophys Acta,
1704,
37-46.
|
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|
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|
|
N.Tuteja,
and
R.Tuteja
(2004).
Unraveling DNA helicases. Motif, structure, mechanism and function.
|
| |
Eur J Biochem,
271,
1849-1863.
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|
O.Cordin,
N.K.Tanner,
M.Doère,
P.Linder,
and
J.Banroques
(2004).
The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity.
|
| |
EMBO J,
23,
2478-2487.
|
|
|
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|
|
P.L.Garcia,
G.Bradley,
C.J.Hayes,
S.Krintel,
P.Soultanas,
and
P.Janscak
(2004).
RPA alleviates the inhibitory effect of vinylphosphonate internucleotide linkages on DNA unwinding by BLM and WRN helicases.
|
| |
Nucleic Acids Res,
32,
3771-3778.
|
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|
|
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|
|
R.Zhao,
J.Shen,
M.R.Green,
M.MacMorris,
and
T.Blumenthal
(2004).
Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export.
|
| |
Structure,
12,
1373-1381.
|
|
|
PDB codes:
|
|
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|
|
|
|
T.Sengoku,
O.Nureki,
N.Dohmae,
A.Nakamura,
and
S.Yokoyama
(2004).
Crystallization and preliminary X-ray analysis of the helicase domains of Vasa complexed with RNA and an ATP analogue.
|
| |
Acta Crystallogr D Biol Crystallogr,
60,
320-322.
|
|
|
|
|
|
|
A.B.Carmel,
and
B.W.Matthews
(2003).
Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein BstDEAD from Bacillus stearothermophilus.
|
| |
Acta Crystallogr D Biol Crystallogr,
59,
1869-1870.
|
|
|
|
|
|
|
D.A.Bernstein,
M.C.Zittel,
and
J.L.Keck
(2003).
High-resolution structure of the E.coli RecQ helicase catalytic core.
|
| |
EMBO J,
22,
4910-4921.
|
|
|
PDB codes:
|
|
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|
|
|
D.Liu,
W.T.Windsor,
and
D.F.Wyss
(2003).
Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2.
|
| |
Protein Sci,
12,
2757-2767.
|
|
|
|
|
|
|
E.A.Worthey,
A.Schnaufer,
I.S.Mian,
K.Stuart,
and
R.Salavati
(2003).
Comparative analysis of editosome proteins in trypanosomatids.
|
| |
Nucleic Acids Res,
31,
6392-6408.
|
|
|
|
|
|
|
N.Sonenberg,
and
T.E.Dever
(2003).
Eukaryotic translation initiation factors and regulators.
|
| |
Curr Opin Struct Biol,
13,
56-63.
|
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|
|
|
|
T.Preiss,
and
M.W Hentze
(2003).
Starting the protein synthesis machine: eukaryotic translation initiation.
|
| |
Bioessays,
25,
1201-1211.
|
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|
|
|
|
|
V.C.Ogilvie,
B.J.Wilson,
S.M.Nicol,
N.A.Morrice,
L.R.Saunders,
G.N.Barber,
and
F.V.Fuller-Pace
(2003).
The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells.
|
| |
Nucleic Acids Res,
31,
1470-1480.
|
|
|
|
|
|
|
J.M.Caruthers,
and
D.B.McKay
(2002).
Helicase structure and mechanism.
|
| |
Curr Opin Struct Biol,
12,
123-133.
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|
L.M.Carastro,
C.K.Tan,
M.Selg,
H.M.Jack,
A.G.So,
and
K.M.Downey
(2002).
Identification of delta helicase as the bovine homolog of HUPF1: demonstration of an interaction with the third subunit of DNA polymerase delta.
|
| |
Nucleic Acids Res,
30,
2232-2243.
|
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|
|
M.C.Ganoza,
M.C.Kiel,
and
H.Aoki
(2002).
Evolutionary conservation of reactions in translation.
|
| |
Microbiol Mol Biol Rev,
66,
460.
|
|
|
|
|
|
|
M.R.Singleton,
and
D.B.Wigley
(2002).
Modularity and specialization in superfamily 1 and 2 helicases.
|
| |
J Bacteriol,
184,
1819-1826.
|
|
|
|
|
|
|
T.M.Hall
(2002).
Poly(A) tail synthesis and regulation: recent structural insights.
|
| |
Curr Opin Struct Biol,
12,
82-88.
|
|
|
|
|
|
|
C.A.Tsu,
K.Kossen,
and
O.C.Uhlenbeck
(2001).
The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA.
|
| |
RNA,
7,
702-709.
|
|
|
|
|
|
|
G.Sianidis,
S.Karamanou,
E.Vrontou,
K.Boulias,
K.Repanas,
N.Kyrpides,
A.S.Politou,
and
A.Economou
(2001).
Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.
|
| |
EMBO J,
20,
961-970.
|
|
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|
M.R.Singleton,
S.Scaife,
and
D.B.Wigley
(2001).
Structural analysis of DNA replication fork reversal by RecG.
|
| |
Cell,
107,
79-89.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
N.K.Tanner,
and
P.Linder
(2001).
DExD/H box RNA helicases: from generic motors to specific dissociation functions.
|
| |
Mol Cell,
8,
251-262.
|
|
|
|
|
|
|
R.M.Story,
H.Li,
and
J.N.Abelson
(2001).
Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii.
|
| |
Proc Natl Acad Sci U S A,
98,
1465-1470.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
W.Li,
and
D.W.Hoffman
(2001).
Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy.
|
| |
Protein Sci,
10,
2426-2438.
|
|
|
PDB code:
|
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|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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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