2V9P

Crystal structure of papillomavirus E1 hexameric helicase DNA-free form

2V9P の概要

• エントリーDOI: 10.2210/pdb2v9p/pdb
• 関連するPDBエントリー: 1F08 1KSX 1KSY 2GXA
• 分子名称: REPLICATION PROTEIN E1, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: aaa+ molecular motor, dna replication, dna translocation, nucleotide-binding, dna-binding, replication, early protein, atpase, nucleus, helicase, hydrolase, atp-binding
• 由来する生物種: BOVINE PAPILLOMAVIRUS TYPE 1
• 細胞内の位置: Host nucleus: P03116
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 417595.50

構造登録者

Sanders, C.M.,Kovalevskiy, O.V.,Sizov, D.,Lebedev, A.A.,Isupov, M.N.,Antson, A.A. (登録日: 2007-08-24, 公開日: 2007-10-02, 最終更新日: 2023-12-13)

主引用文献

Sanders, C.M.,Kovalevskiy, O.V.,Sizov, D.,Lebedev, A.A.,Isupov, M.N.,Antson, A.A.
Papillomavirus E1 Helicase Assembly Maintains an Asymmetric State in the Absence of DNA and Nucleotide Cofactors.
Nucleic Acids Res., 35:6451-, 2007

PubMed Abstract: Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first time observed in the absence of nucleotide cofactors and DNA. Surprisingly, the ATP-binding sites adopt specific conformations linked to positional changes in the DNA-binding hairpins, which follow a wave-like trajectory, as observed previously in the E1/DNA/ADP complex. The protein's assembly thus maintains such an asymmetric state in the absence of DNA and nucleotide cofactors, allowing consideration of the E1 helicase action as the propagation of a conformational wave around the protein ring. The data imply that the wave's propagation within the AAA+ domains is not necessarily coupled with a strictly sequential hydrolysis of ATP. Since a single ATP hydrolysis event would affect the whole hexamer, such events may simply serve to rectify the direction of the wave's motion.

PubMed: 17881379
DOI: 10.1093/NAR/GKM705

実験手法

X-RAY DIFFRACTION (3 Å)