5NWT

Crystal Structure of Escherichia coli RNA polymerase - Sigma54 Holoenzyme complex

「5BYH」から置き換えられました

5NWT の概要

• エントリーDOI: 10.2210/pdb5nwt/pdb
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
• 機能のキーワード: sigma 54, rna polymerase, holoenzyme, transcription, transferase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 440882.32

構造登録者

Zhang, X.,Buck, M.,Darbari, V.C.,Yang, Y.,Zhang, N.,Lu, D.,Glyde, R.,Wang, Y.,Winkelman, J.,Gourse, R.L.,Murakami, K.S. (登録日: 2017-05-08, 公開日: 2017-09-13, 最終更新日: 2024-10-23)

主引用文献

Yang, Y.,Darbari, V.C.,Zhang, N.,Lu, D.,Glyde, R.,Wang, Y.P.,Winkelman, J.T.,Gourse, R.L.,Murakami, K.S.,Buck, M.,Zhang, X.
TRANSCRIPTION. Structures of the RNA polymerase-Sigma54 reveal new and conserved regulatory strategies.
Science, 349:882-885, 2015

PubMed Abstract: Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by σ factors. The major variant σ factor (σ(54)) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate-dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-σ(54) holoenzyme at 3.8 angstroms reveals molecular details of σ(54) and its interactions with RNAP. The structure explains how σ(54) targets different regions in RNAP to exert its inhibitory function. Although σ(54) and the major σ factor, σ(70), have similar functional domains and contact similar regions of RNAP, unanticipated differences are observed in their domain arrangement and interactions with RNAP, explaining their distinct properties. Furthermore, we observe evolutionarily conserved regulatory hotspots in RNAPs that can be targeted by a diverse range of mechanisms to fine tune transcription.

PubMed: 26293966
DOI: 10.1126/science.aab1478

実験手法

X-RAY DIFFRACTION (3.76 Å)