3SEO

Crystal structure of VopL C terminal domain

Summary for 3SEO

• Entry DOI: 10.2210/pdb3seo/pdb
• Descriptor: VopL C terminal domain protein, CHLORIDE ION (3 entities in total)
• Functional Keywords: alpha helix, structural protein
• Biological source: Vibrio parahaemolyticus
• Total number of polymer chains: 2
• Total formula weight: 53979.37

Authors

Yu, B.,Rosen, M.K.,Tomchick, D.R. (deposition date: 2011-06-10, release date: 2011-08-31, Last modification date: 2024-02-28)

Primary citation

Yu, B.,Cheng, H.C.,Brautigam, C.A.,Tomchick, D.R.,Rosen, M.K.
Mechanism of actin filament nucleation by the bacterial effector VopL.
Nat.Struct.Mol.Biol., 18:1068-1074, 2011

PubMed Abstract: 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.

PubMed: 21873984
DOI: 10.1038/nsmb.2110

Experimental method

X-RAY DIFFRACTION (2.305 Å)