3ryl | pdb_00003ryl

Dimerization domain of Vibrio parahemolyticus VopL

spinqualitylabelsall models 3ryl, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ryl is a 2 chain structure with sequence from Vibrio parahaemolyticus RIMD 2210633. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q87GE5_VIBPA Publication Abstract from PubMed 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. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation.,Namgoong S, Boczkowska M, Glista MJ, Winkelman JD, Rebowski G, Kovar DR, Dominguez R Nat Struct Mol Biol. 2011 Aug 28;18(9):1060-7. doi: 10.1038/nsmb.2109. PMID:21873985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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