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PDBsum entry 4gzy
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Transcription/DNA/RNA
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PDB id
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4gzy
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Contents |
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223 a.a.
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1083 a.a.
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1358 a.a.
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93 a.a.
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PDB id:
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Transcription/DNA/RNA
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Title:
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Crystal structures of bacterial RNA polymerase paused elongation complexes
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Structure:
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DNA-directed RNA polymerase subunit alpha. Chain: a, b. Synonym: rnap subunit alpha, RNA polymerase subunit alpha, transcriptase subunit alpha. Engineered: yes. DNA-directed RNA polymerase subunit beta. Chain: c. Synonym: rnap subunit beta, RNA polymerase subunit beta, transcriptase subunit beta.
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Source:
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Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Gene: rpoa, ttha1664. Expressed in: thermus thermophilus. Expression_system_taxid: 274. Gene: rpob, ttha1813. Gene: rpoc, ttha1812. Gene: rpoz, ttha1561.
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Resolution:
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3.51Å
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R-factor:
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0.266
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R-free:
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0.322
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Authors:
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A.Weixlbaumer,K.Leon,R.Landick,S.A.Darst
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Key ref:
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A.Weixlbaumer
et al.
(2013).
Structural basis of transcriptional pausing in bacteria.
Cell,
152,
431-441.
PubMed id:
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Date:
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06-Sep-12
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Release date:
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13-Feb-13
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PROCHECK
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Headers
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References
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Q5SHR6
(RPOA_THET8) -
DNA-directed RNA polymerase subunit alpha from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq: Struc:
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315 a.a.
223 a.a.
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Q8RQE9
(RPOB_THET8) -
DNA-directed RNA polymerase subunit beta from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq: Struc:
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1119 a.a.
1083 a.a.
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Enzyme class:
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Chains A, B, C, D, E:
E.C.2.7.7.6
- DNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Cell
152:431-441
(2013)
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PubMed id:
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Structural basis of transcriptional pausing in bacteria.
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A.Weixlbaumer,
K.Leon,
R.Landick,
S.A.Darst.
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ABSTRACT
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Transcriptional pausing by multisubunit RNA polymerases (RNAPs) is a key
mechanism for regulating gene expression in both prokaryotes and eukaryotes and
is a prerequisite for transcription termination. Pausing and termination states
are thought to arise through a common, elemental pause state that is inhibitory
for nucleotide addition. We report three crystal structures of Thermus RNAP
elemental paused elongation complexes (ePECs). The structures reveal the same
relaxed, open-clamp RNAP conformation in the ePEC that may arise by failure to
re-establish DNA contacts during translocation. A kinked bridge-helix sterically
blocks the RNAP active site, explaining how this conformation inhibits RNAP
catalytic activity. Our results provide a framework for understanding how RNA
hairpin formation stabilizes the paused state and how the ePEC intermediate
facilitates termination.
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');
}
}
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