4YG2

X-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzyme

「4IGC」から置き換えられました

4YG2 の概要

• エントリーDOI: 10.2210/pdb4yg2/pdb
• 関連するPDBエントリー: 4IGC 4YFK 4YFN 4YFX
• 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: rna polymerase, transferase-transcription complex, transferase/transcription
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 920172.47

構造登録者

Murakami, K.S. (登録日: 2015-02-25, 公開日: 2015-03-18, 最終更新日: 2024-02-28)

主引用文献

Murakami, K.S.
X-ray crystal structure of Escherichia coli RNA polymerase sigma70 holoenzyme
J. Biol. Chem., 288:9126-9134, 2013

PubMed Abstract: Escherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual domains. Here, I report the x-ray structure of the E. coli RNAP σ(70) holoenzyme, which shows σ region 1.1 (σ1.1) and the α subunit C-terminal domain for the first time in the context of an intact RNAP. σ1.1 is positioned at the RNAP DNA-binding channel and completely blocks DNA entry to the RNAP active site. The structure reveals that σ1.1 contains a basic patch on its surface, which may play an important role in DNA interaction to facilitate open promoter complex formation. The α subunit C-terminal domain is positioned next to σ domain 4 with a fully stretched linker between the N- and C-terminal domains. E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs.

PubMed: 23389035
DOI: 10.1074/jbc.M112.430900

実験手法

X-RAY DIFFRACTION (3.7 Å)