6X50

Mfd-bound E.coli RNA polymerase elongation complex - V state

6X50 の概要

• エントリーDOI: 10.2210/pdb6x50/pdb
• 関連するPDBエントリー: 6X26 6X2F 6X2N 6X43 6X4W 6X4Y
• EMDBエントリー: 21996 22006 22012 22039 22043 22044 22045
• 分子名称: Transcription-repair-coupling factor, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• 機能のキーワード: transcription-coupled dna repair, dna translocase, elongation complex, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna
• 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: 566282.69

構造登録者

Llewelyn, E.,Chen, J.,Kang, J.Y.,Darst, S.A. (登録日: 2020-05-24, 公開日: 2021-02-03, 最終更新日: 2025-05-14)

主引用文献

Kang, J.Y.,Llewellyn, E.,Chen, J.,Olinares, P.D.B.,Brewer, J.,Chait, B.T.,Campbell, E.A.,Darst, S.A.
Structural basis for transcription complex disruption by the Mfd translocase.
Elife, 10:-, 2021

PubMed Abstract: Transcription-coupled repair (TCR) is a sub-pathway of nucleotide excision repair (NER) that preferentially removes lesions from the template-strand (t-strand) that stall RNA polymerase (RNAP) elongation complexes (ECs). Mfd mediates TCR in bacteria by removing the stalled RNAP concealing the lesion and recruiting Uvr(A)BC. We used cryo-electron microscopy to visualize Mfd engaging with a stalled EC and attempting to dislodge the RNAP. We visualized seven distinct Mfd-EC complexes in both ATP and ADP-bound states. The structures explain how Mfd is remodeled from its repressed conformation, how the UvrA-interacting surface of Mfd is hidden during most of the remodeling process to prevent premature engagement with the NER pathway, how Mfd alters the RNAP conformation to facilitate disassembly, and how Mfd forms a processive translocation complex after dislodging the RNAP. Our results reveal an elaborate mechanism for how Mfd kinetically discriminates paused from stalled ECs and disassembles stalled ECs to initiate TCR.

PubMed: 33480355
DOI: 10.7554/eLife.62117

実験手法

ELECTRON MICROSCOPY (3.3 Å)