4GZZ

Crystal structures of bacterial RNA Polymerase paused elongation complexes

Summary for 4GZZ

• Entry DOI: 10.2210/pdb4gzz/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total)
• Functional Keywords: rna polymerase, transcription, paused transcription elongation complex, transcriptional pausing, dna directed rna transcription', transcription-dna-rna hybrid complex, transcription/dna-rna hybrid
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 8
• Total formula weight: 395444.15

Authors

Weixlbaumer, A.,Leon, K.,Landick, R.,Darst, S.A. (deposition date: 2012-09-06, release date: 2013-02-13, Last modification date: 2023-09-13)

Primary citation

Weixlbaumer, A.,Leon, K.,Landick, R.,Darst, S.A.
Structural basis of transcriptional pausing in bacteria.
Cell(Cambridge,Mass.), 152:431-441, 2013

PubMed Abstract: 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.

PubMed: 23374340
DOI: 10.1016/j.cell.2012.12.020

Experimental method

X-RAY DIFFRACTION (4.2927 Å)