3onx

Crystal structure of a domain of a protein involved in formation of actin cytoskeleton

spinqualitylabelsall models 3onx, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3onx is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.904Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BUD6_YEAST Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton. Publication Abstract from PubMed Formin proteins and their associated factors cooperate to assemble unbranched actin filaments in diverse cellular structures. The Saccharomyces cerevisiae formin Bni1 and its associated nucleation-promoting factor (NPF) Bud6 generate actin cables and mediate polarized cell growth. Bud6 binds to both the tail of the formin and G-actin, thereby recruiting monomeric actin to the formin to create a nucleation seed. Here, we structurally and functionally dissect the nucleation-promoting C-terminal region of Bud6 into a Bni1-binding "core" domain and a G-actin binding "flank" domain. The approximately 2-A resolution crystal structure of the Bud6 core domain reveals an elongated dimeric rod with a unique fold resembling a triple-helical coiled-coil. Binding and actin-assembly assays show that conserved residues on the surface of this domain mediate binding to Bni1 and are required for NPF activity. We find that the Bni1 dimer binds two Bud6 dimers and that the Bud6 flank binds a single G-actin molecule. These findings suggest a model in which a Bni1/Bud6 complex with a 2:4 subunit stoichiometry assembles a nucleation seed with Bud6 coordinating up to four actin subunits. Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6.,Tu D, Graziano BR, Park E, Zheng W, Li Y, Goode BL, Eck MJ Proc Natl Acad Sci U S A. 2012 Nov 16. PMID:23161908 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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