4M63

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

Summary for 4M63

• Entry DOI: 10.2210/pdb4m63/pdb
• Descriptor: T3SS2 effector VopL nucleation of actin polymerization, Actin-5C, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: actin nucleator, actin nucleation, hydrolase, wasp homology 2 domain, vopl c-terminal domain, cytoskeleton, atp-binding protein, actin-binding protein
• Biological source: Vibrio parahaemolyticus; More
• Cellular location: Cytoplasm, cytoskeleton: P10987
• Total number of polymer chains: 5
• Total formula weight: 180700.27

Authors

Tomchick, D.R.,Zahm, J.A.,Rosen, M.K. (deposition date: 2013-08-08, release date: 2013-10-23, Last modification date: 2023-09-20)

Primary citation

Zahm, J.A.,Padrick, S.B.,Chen, Z.,Pak, C.W.,Yunus, A.A.,Henry, L.,Tomchick, D.R.,Chen, Z.,Rosen, M.K.
The Bacterial Effector VopL Organizes Actin into Filament-like Structures.
Cell(Cambridge,Mass.), 155:423-434, 2013

PubMed 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.

PubMed: 24120140
DOI: 10.1016/j.cell.2013.09.019

Experimental method

X-RAY DIFFRACTION (2.748 Å)