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PDBsum entry 1m1h
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Transcription
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PDB id
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1m1h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of transcription factor nusg in light of its nucleic acid- And protein-Binding activities.
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Authors
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T.Steiner,
J.T.Kaiser,
S.Marinkoviç,
R.Huber,
M.C.Wahl.
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Ref.
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EMBO J, 2002,
21,
4641-4653.
[DOI no: ]
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PubMed id
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Abstract
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Microbial transcription modulator NusG interacts with RNA polymerase and
termination factor rho, displaying striking functional homology to eukaryotic
Spt5. The protein is also a translational regulator. We have determined crystal
structures of Aquifex aeolicus NusG showing a modular design: an N-terminal
RNP-like domain, a C-terminal element with a KOW sequence motif and a
species-specific immunoglobulin-like fold. The structures reveal bona fide
nucleic acid binding sites, and nucleic acid binding activities can be detected
for NusG from three organisms and for the KOW element alone. A conserved KOW
domain is defined as a new class of nucleic acid binding folds. This module is a
close structural homolog of tudor protein-protein interaction motifs. Putative
protein binding sites for the RNP and KOW domains can be deduced, which differ
from the areas implicated in nucleic acid interactions. The results strongly
argue that both protein and nucleic acid contacts are important for NusG's
functions and that the factor can act as an adaptor mediating indirect
protein-nucleic acid associations.
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Figure 4.
Figure 4 (A) Superposition of aaeNusG domain III (gold),
r-protein L24 (blue) and the SMN tudor domain (red). F211 of
aaeNusG and Y109 of the tudor domain, presumably important for
contacting other proteins, are shown in ball-and-stick. (B)
Domain III in complex with RNA molecules according to the
L24−rRNA structure. The sequence originally identified as the
KOW element is shown in red.
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Figure 6.
Figure 6 (A) Deduced nucleic acid (brown) and protein (green)
interaction sites mapped onto the aaeNusG surface. The left
panel is in the same orientation as Figure 2C. The three domains
are labeled. Numbers identify potential interactions sites. 1,
S6-like nucleic acid interaction site; 2, U1A-like nucleic acid
interaction site; 3, nucleic acid interaction site mapped by
L24−rRNA contacts; 4, S18-like protein interaction site; 5,
tudor-like protein interaction site. If helix  3
of the RNP motif was removed upon U1A-like nucleic acid
interaction, additional contact sites would become uncovered.
Interaction sites that could not be deduced from the structures
may also exist in domain II. (B) Stereo-ribbon plot of aaeNusG
with the mutated residues in magenta (with phenotype) and light
blue (no phenotype).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2002,
21,
4641-4653)
copyright 2002.
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