Journal
CELL
Volume 155, Issue 2, Pages 423-434Publisher
CELL PRESS
DOI: 10.1016/j.cell.2013.09.019
Keywords
-
Categories
Funding
- Howard Hughes Medical Institute
- NIH [R01-GM56322]
- Welch Foundation [I-1544]
- U.S. Department of Energy Office of Biological and Environmental Research [DE-AC02-06CH11357]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available