3RYL

Dimerization domain of Vibrio parahemolyticus VopL

Summary for 3RYL

• Entry DOI: 10.2210/pdb3ryl/pdb
• Descriptor: protein VPA1370 (1 entity in total)
• Functional Keywords: actin nucleation, filament pointed end binding, type iii secretion system (t3ss) protein, protein binding
• Biological source: Vibrio parahaemolyticus
• Total number of polymer chains: 2
• Total formula weight: 54129.25

Authors

Namgoong, S.,Dominguez, R. (deposition date: 2011-05-11, release date: 2011-08-31, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)