3BH0

ATPase Domain of G40P

3BH0 の概要

• エントリーDOI: 10.2210/pdb3bh0/pdb
• 関連するPDBエントリー: 3BGW
• 分子名称: DNAB-LIKE REPLICATIVE HELICASE (2 entities in total)
• 機能のキーワード: helicase, atpase, replication
• 由来する生物種: Bacillus phage SPP1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35524.04

構造登録者

Wang, G.,Klein, M.G.,Tokonzaba, E.,Zhang, Y.,Holden, L.G.,Chen, X.S. (登録日: 2007-11-27, 公開日: 2007-12-25, 最終更新日: 2024-02-21)

主引用文献

Wang, G.,Klein, M.G.,Tokonzaba, E.,Zhang, Y.,Holden, L.G.,Chen, X.S.
The structure of a DnaB-family replicative helicase and its interactions with primase.
Nat.Struct.Mol.Biol., 15:94-100, 2008

PubMed Abstract: Helicases are essential enzymes for DNA replication, a fundamental process in all living organisms. The DnaB family are hexameric replicative helicases that unwind duplex DNA and coordinate with RNA primase and other proteins at the replication fork in prokaryotes. Here, we report the full-length crystal structure of G40P, a DnaB family helicase. The hexamer complex reveals an unusual architectural feature and a new type of assembly mechanism. The hexamer has two tiers: a three-fold symmetric N-terminal tier and a six-fold symmetric C-terminal tier. Monomers with two different conformations, termed cis and trans, come together to provide a topological solution for the dual symmetry within a hexamer. Structure-guided mutational studies indicate an important role for the N-terminal tier in binding primase and regulating primase-mediated stimulation of helicase activity. This study provides insights into the structural and functional interplay between G40P helicase and DnaG primase.

PubMed: 18157148
DOI: 10.1038/nsmb1356

実験手法

X-RAY DIFFRACTION (2.35 Å)