7APD

Bovine Papillomavirus E1 DNA helicase-replication fork complex

7APD の概要

• エントリーDOI: 10.2210/pdb7apd/pdb
• EMDBエントリー: 11852
• 分子名称: Replication protein E1, DNA (40-MER), DNA (36-MER), ... (4 entities in total)
• 機能のキーワード: dna, virus, helicase, replisome, dna replication., dna binding protein
• 由来する生物種: Bovine papillomavirus; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 260702.07

構造登録者

Javed, A.,Major, B.,Stead, J.,Sanders, C.M.,Orlova, E.V. (登録日: 2020-10-16, 公開日: 2021-11-17, 最終更新日: 2024-07-10)

主引用文献

Javed, A.,Major, B.,Stead, J.A.,Sanders, C.M.,Orlova, E.V.
Unwinding of a DNA replication fork by a hexameric viral helicase.
Nat Commun, 12:5535-5535, 2021

PubMed Abstract: Hexameric helicases are motor proteins that unwind double-stranded DNA (dsDNA) during DNA replication but how they are optimised for strand separation is unclear. Here we present the cryo-EM structure of the full-length E1 helicase from papillomavirus, revealing all arms of a bound DNA replication fork and their interactions with the helicase. The replication fork junction is located at the entrance to the helicase collar ring, that sits above the AAA + motor assembly. dsDNA is escorted to and the 5´ single-stranded DNA (ssDNA) away from the unwinding point by the E1 dsDNA origin binding domains. The 3´ ssDNA interacts with six spirally-arranged β-hairpins and their cyclical top-to-bottom movement pulls the ssDNA through the helicase. Pulling of the RF against the collar ring separates the base-pairs, while modelling of the conformational cycle suggest an accompanying movement of the collar ring has an auxiliary role, helping to make efficient use of ATP in duplex unwinding.

PubMed: 34545080
DOI: 10.1038/s41467-021-25843-6

実験手法

ELECTRON MICROSCOPY (3.9 Å)