The bacterial effector VopL organizes actin into filament-like structures.

Abstract:

:VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. 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.

journal_name

Cell

journal_title

Cell

authors

Zahm JA,Padrick SB,Chen Z,Pak CW,Yunus AA,Henry L,Tomchick DR,Chen Z,Rosen MK

doi

10.1016/j.cell.2013.09.019

subject

Has Abstract

pub_date

2013-10-10 00:00:00

pages

423-34

issue

2

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(13)01156-2

journal_volume

155

pub_type

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