Logo image
Structure of a Filament-Like Actin Trimer Bound to the Bacterial Effector VopL
Journal article   Open access   Peer reviewed

Structure of a Filament-Like Actin Trimer Bound to the Bacterial Effector VopL

Jacob A. Zahm, Shae B. Padrick, Zhucheng Chen, Chi W. Pak, Ali A. Yunus, Lisa Henry, Diana R. Tomchick, Zhe Chen and Michael K. Rosen
Cell, v 155(2), pp 423-434
10 Oct 2013
PMID: 24120140
url
https://doi.org/10.1016/j.cell.2013.09.019View
Published, Version of Record (VoR) Open

Abstract

Bacterial pathogens use secreted effector proteins to subvert host-cell defenses. VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal Domain (VCD) and a tandem array of three WASP homology 2 (WH2) motifs. Here we report the crystal structure of the VCD dimer bound to actin. The VCD binds three actin monomers in a spatial arrangement close to that in the canonical actin filament. In this configuration each actin can readily accommodate a WH2 motif. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD and delivered by the WH2 array, that can template addition of new monomers. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation.

Metrics

10 Record Views
42 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
Logo image