3RYL

Dimerization domain of Vibrio parahemolyticus VopL

3RYL の概要

• エントリーDOI: 10.2210/pdb3ryl/pdb
• 分子名称: protein VPA1370 (1 entity in total)
• 機能のキーワード: actin nucleation, filament pointed end binding, type iii secretion system (t3ss) protein, protein binding
• 由来する生物種: Vibrio parahaemolyticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54129.25

構造登録者

Namgoong, S.,Dominguez, R. (登録日: 2011-05-11, 公開日: 2011-08-31, 最終更新日: 2024-10-30)

主引用文献

Namgoong, S.,Boczkowska, M.,Glista, M.J.,Winkelman, J.D.,Rebowski, G.,Kovar, D.R.,Dominguez, R.
Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation.
Nat.Struct.Mol.Biol., 18:1060-1067, 2011

PubMed Abstract: Pathogen proteins targeting the actin cytoskeleton often serve as model systems to understand their more complex eukaryotic analogs. We show that the strong actin filament nucleation activity of Vibrio parahaemolyticus VopL depends on its three W domains and on its dimerization through a unique VopL C-terminal domain (VCD). The VCD shows a previously unknown all-helical fold and interacts with the pointed end of the actin nucleus, contributing to the nucleation activity directly and through duplication of the W domain repeat. VopL promotes rapid cycles of filament nucleation and detachment but generally has no effect on elongation. Profilin inhibits VopL-induced nucleation by competing for actin binding to the W domains. Combined, the results suggest that VopL stabilizes a hexameric double-stranded pointed end nucleus. Analysis of hybrid constructs of VopL and the eukaryotic nucleator Spire suggest that Spire may also function as a dimer in cells.

PubMed: 21873985
DOI: 10.1038/nsmb.2109

実験手法

X-RAY DIFFRACTION (3.1 Å)