4GZZ
Crystal structures of bacterial RNA Polymerase paused elongation complexes
4GZZ の概要
エントリーDOI | 10.2210/pdb4gzz/pdb |
分子名称 | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total) |
機能のキーワード | rna polymerase, transcription, paused transcription elongation complex, transcriptional pausing, dna directed rna transcription', transcription-dna-rna hybrid complex, transcription/dna-rna hybrid |
由来する生物種 | Thermus thermophilus 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 395444.15 |
構造登録者 | Weixlbaumer, A.,Leon, K.,Landick, R.,Darst, S.A. (登録日: 2012-09-06, 公開日: 2013-02-13, 最終更新日: 2023-09-13) |
主引用文献 | Weixlbaumer, A.,Leon, K.,Landick, R.,Darst, S.A. Structural basis of transcriptional pausing in bacteria. Cell(Cambridge,Mass.), 152:431-441, 2013 Cited by 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: 23374340DOI: 10.1016/j.cell.2012.12.020 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (4.2927 Å) |
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