Structural highlights
4gzy is a 8 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Gene: | rpoA, TTHA1664 (Thermus thermophilus HB8), rpoB, TTHA1813 (Thermus thermophilus HB8), rpoC, TTHA1812 (Thermus thermophilus HB8), rpoZ, TTHA1561 (Thermus thermophilus HB8) |
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[RPOZ_THET8] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). [RPOA_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [RPOC_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [RPOB_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Publication Abstract from PubMed
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.
Structural basis of transcriptional pausing in bacteria.,Weixlbaumer A, Leon K, Landick R, Darst SA Cell. 2013 Jan 31;152(3):431-41. doi: 10.1016/j.cell.2012.12.020. PMID:23374340[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weixlbaumer A, Leon K, Landick R, Darst SA. Structural basis of transcriptional pausing in bacteria. Cell. 2013 Jan 31;152(3):431-41. doi: 10.1016/j.cell.2012.12.020. PMID:23374340 doi:http://dx.doi.org/10.1016/j.cell.2012.12.020
