1svy | pdb_00001svy

SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE

spinqualitylabelsall models 1svy, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1svy is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: CA, CSO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SEVE_DICDI Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of the F-actin binding domain 2 of severin, the gelsolin homologue from Dictyostelium discoideum, has been determined by multiple isomorphous replacement and refined to 1.75 A resolution. The structure reveals an alpha-helix-beta-sheet sandwich similar to the domains of gelsolin and villin, and contains two cation-binding sites, as observed in other domain 1 and domain 2 homologues. Comparison of the structures of several gelsolin family domains has identified residues that may mediate F-actin binding in gelsolin domain 2 homologues. To assess the involvement of these residues in F-actin binding, three mutants of human gelsolin domain 2 were assayed for F-actin binding activity and thermodynamic stability. Two of the mutants, RRV168AAA and RLK210AAA, demonstrated a lowered affinity for F-actin, indicating a role for those residues in filament binding. Using both structural and biochemical data, we have constructed a model of the gelsolin domain 1-domain 2-F-actin complex. This model highlights a number of interactions that may serve as positive and negative determinants of filament end- and side-binding. Mapping the functional surface of domain 2 in the gelsolin superfamily.,Puius YA, Fedorov EV, Eichinger L, Schleicher M, Almo SC Biochemistry. 2000 May 9;39(18):5322-31. PMID:10820002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Severin

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