7M8E

E.coli RNAP-RapA elongation complex

7M8E の概要

• エントリーDOI: 10.2210/pdb7m8e/pdb
• EMDBエントリー: 23716
• 分子名称: DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• 機能のキーワード: swi2/snf2, rapa, atpase, rna polymerase, transferase-hydrolase-dna-rna complex, transferase/hydrolase/dna/rna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 528428.87

構造登録者

Shi, W.,Liu, B. (登録日: 2021-03-29, 公開日: 2021-08-18, 最終更新日: 2024-05-29)

主引用文献

Shi, W.,Zhou, W.,Chen, M.,Yang, Y.,Hu, Y.,Liu, B.
Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.
Nucleic Acids Res., 49:10707-10716, 2021

PubMed Abstract: RapA is a bacterial RNA polymerase (RNAP)-associated Swi2/Snf2 ATPase that stimulates RNAP recycling. The ATPase activity of RapA is autoinhibited by its N-terminal domain (NTD) but activated with RNAP bound. Here, we report a 3.4-Å cryo-EM structure of Escherichia coli RapA-RNAP elongation complex, in which the ATPase active site of RapA is structurally remodeled. In this process, the NTD of RapA is wedged open by RNAP β' zinc-binding domain (ZBD). In addition, RNAP β flap tip helix (FTH) forms extensive hydrophobic interactions with RapA ATPase core domains. Functional assay demonstrates that removing the ZBD or FTH of RNAP significantly impairs its ability to activate the ATPase activity of RapA. Our results provide the structural basis of RapA ATPase activation by RNAP, through the active site remodeling driven by the ZBD-buttressed large-scale opening of NTD and the direct interactions between FTH and ATPase core domains.

PubMed: 34428297
DOI: 10.1093/nar/gkab744

実験手法

ELECTRON MICROSCOPY (3.4 Å)