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PDBsum entry 1l2f
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Transcription
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PDB id
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1l2f
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
42:13429-13437
(2003)
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PubMed id:
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Crystal structure of NusA from Thermotoga maritima and functional implication of the N-terminal domain.
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D.H.Shin,
H.H.Nguyen,
J.Jancarik,
H.Yokota,
R.Kim,
S.H.Kim.
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ABSTRACT
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We report the crystal structure of N-utilizing substance A protein (NusA) from
Thermotoga maritima (TmNusA), a protein involved in transcriptional pausing,
termination, and antitermination. TmNusA has an elongated rod-shaped structure
consisting of an N-terminal domain (NTD, residues 1-132) and three RNA binding
domains (RBD). The NTD consists of two subdomains, the globular head and the
helical body domains, that comprise a unique three-dimensional structure that
may be important for interacting with RNA polymerase. The globular head domain
possesses a high content of negatively charged residues that may interact with
the positively charged flaplike domain of RNA polymerase. The helical body
domain is composed of a three-helix bundle that forms a hydrophobic core with
the aid of two neighboring beta-strands. This domain shows structural similarity
with one of the helical domains of sigma(70) factor from Escherichia coli. One
side of the molecular surface shows positive electrostatic potential suitable
for nonspecific RNA interaction. The RBD is composed of one S1 domain and two
K-homology (KH) domains forming an elongated RNA binding surface. Structural
comparison between TmNusA and Mycobacterium tuberculosis NusA reveals a possible
hinge motion between NTD and RBD. In addition, a functional implication of the
NTD in its interaction with RNA polymerase is discussed.
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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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T.C.Terwilliger
(2010).
Rapid model building of alpha-helices in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
268-275.
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T.C.Terwilliger
(2010).
Rapid model building of beta-sheets in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
276-284.
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T.C.Terwilliger
(2010).
Rapid chain tracing of polypeptide backbones in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
285-294.
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S.E.Cohen,
V.G.Godoy,
and
G.C.Walker
(2009).
Transcriptional modulator NusA interacts with translesion DNA polymerases in Escherichia coli.
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J Bacteriol,
191,
665-672.
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K.B.Arnvig,
S.Zeng,
S.Quan,
A.Papageorge,
N.Zhang,
A.C.Villapakkam,
and
C.L.Squires
(2008).
Evolutionary comparison of ribosomal operon antitermination function.
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J Bacteriol,
190,
7251-7257.
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O.Paliy,
S.M.Gargac,
Y.Cheng,
V.N.Uversky,
and
A.K.Dunker
(2008).
Protein disorder is positively correlated with gene expression in Escherichia coli.
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J Proteome Res,
7,
2234-2245.
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A.Eisenmann,
S.Schwarz,
S.Prasch,
K.Schweimer,
and
P.Rösch
(2005).
The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction.
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Protein Sci,
14,
2018-2029.
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PDB codes:
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B.Beuth,
S.Pennell,
K.B.Arnvig,
S.R.Martin,
and
I.A.Taylor
(2005).
Structure of a Mycobacterium tuberculosis NusA-RNA complex.
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EMBO J,
24,
3576-3587.
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PDB codes:
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S.Borukhov,
J.Lee,
and
O.Laptenko
(2005).
Bacterial transcription elongation factors: new insights into molecular mechanism of action.
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Mol Microbiol,
55,
1315-1324.
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D.H.Shin,
Y.Lou,
J.Jancarik,
H.Yokota,
R.Kim,
and
S.H.Kim
(2004).
Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain.
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Proc Natl Acad Sci U S A,
101,
13198-13203.
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PDB code:
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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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