6M6B

Cryo-EM structure of Thermus thermophilus Mfd in complex with RNA polymerase and ATP-gamma-S

6M6B の概要

• エントリーDOI: 10.2210/pdb6m6b/pdb
• EMDBエントリー: 30118
• 分子名称: DNA-directed RNA polymerase subunit alpha, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• 機能のキーワード: transcription, rna polymerase, dna repair, mfd
• 由来する生物種: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 527288.78

構造登録者

Shi, J.,Wen, A.,Feng, Y. (登録日: 2020-03-14, 公開日: 2020-10-14, 最終更新日: 2025-06-18)

主引用文献

Shi, J.,Wen, A.,Zhao, M.,Jin, S.,You, L.,Shi, Y.,Dong, S.,Hua, X.,Zhang, Y.,Feng, Y.
Structural basis of Mfd-dependent transcription termination.
Nucleic Acids Res., 48:11762-11772, 2020

PubMed Abstract: Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite extensive studies, the molecular mechanism of Mfd-dependent transcription termination in bacteria remains unclear, with several long-standing puzzles. How Mfd is activated by stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA are unknown. Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes profound conformational changes upon activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP clamp. These structures provide a foundation for future studies aimed at dissecting the precise mechanism of Mfd-dependent transcription termination and pave the way for rational drug design targeting Mfd for the purpose of tackling the antimicrobial resistance crisis.

PubMed: 33068413
DOI: 10.1093/nar/gkaa904

実験手法

ELECTRON MICROSCOPY (4.1 Å)