3seo | pdb_00003seo

Crystal structure of VopL C terminal domain

spinqualitylabelsall models 3seo, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3seo is a 2 chain structure with sequence from "oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Gene: VopL, VPA1370 ("Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Vibrio parahaemolyticus protein L (VopL) is an actin nucleation factor that induces stress fibers when injected into eukaryotic host cells. VopL contains three N-terminal Wiskott-Aldrich homology 2 (WH2) motifs and a unique VopL C-terminal domain (VCD). We describe crystallographic and biochemical analyses of filament nucleation by VopL. The WH2 element of VopL does not nucleate on its own and requires the VCD for activity. The VCD forms a U-shaped dimer in the crystal, stabilized by a terminal coiled coil. Dimerization of the WH2 motifs contributes strongly to nucleation activity, as do contacts of the VCD to actin. Our data lead to a model in which VopL stabilizes primarily lateral (short-pitch) contacts between actin monomers to create the base of a two-stranded filament. Stabilization of lateral contacts may be a common feature of actin filament nucleation by WH2-based factors. Mechanism of actin filament nucleation by the bacterial effector VopL.,Yu B, Cheng HC, Brautigam CA, Tomchick DR, Rosen MK Nat Struct Mol Biol. 2011 Aug 28;18(9):1068-74. doi: 10.1038/nsmb.2110. PMID:21873984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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