6XEO

Structure of Mfd bound to dsDNA

6XEO の概要

• エントリーDOI: 10.2210/pdb6xeo/pdb
• EMDBエントリー: 22146
• 分子名称: Transcription-repair-coupling factor, DNA (5'-D(P*AP*GP*GP*AP*TP*AP*CP*TP*TP*AP*CP*AP*GP*CP*CP*AP*TP*C)-3'), DNA (5'-D(P*GP*AP*TP*GP*GP*CP*TP*GP*TP*AP*AP*GP*TP*AP*TP*CP*CP*T)-3') (3 entities in total)
• 機能のキーワード: dna translocase, transcription-coupled dna repair, helicase, atpase, dna binding protein, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 144501.85

構造登録者

Brugger, C.,Deaconescu, A. (登録日: 2020-06-12, 公開日: 2020-08-19, 最終更新日: 2024-03-06)

主引用文献

Brugger, C.,Zhang, C.,Suhanovsky, M.M.,Kim, D.D.,Sinclair, A.N.,Lyumkis, D.,Deaconescu, A.M.
Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd.
Nat Commun, 11:3740-3740, 2020

PubMed Abstract: Mfd couples transcription to nucleotide excision repair, and acts on RNA polymerases when elongation is impeded. Depending on impediment severity, this action results in either transcription termination or elongation rescue, which rely on ATP-dependent Mfd translocation on DNA. Due to its role in antibiotic resistance, Mfd is also emerging as a prime target for developing anti-evolution drugs. Here we report the structure of DNA-bound Mfd, which reveals large DNA-induced structural changes that are linked to the active site via ATPase motif VI. These changes relieve autoinhibitory contacts between the N- and C-termini and unmask UvrA recognition determinants. We also demonstrate that translocation relies on a threonine in motif Ic, widely conserved in translocases, and a family-specific histidine near motif IVa, reminiscent of the "arginine clamp" of RNA helicases. Thus, Mfd employs a mode of DNA recognition that at its core is common to ss/ds translocases that act on DNA or RNA.

PubMed: 32719356
DOI: 10.1038/s41467-020-17457-1

実験手法

ELECTRON MICROSCOPY (5.5 Å)