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1svy
From Proteopedia
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SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE
Overview
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.
About this Structure
1SVY is a Single protein structure of sequence from Dictyostelium discoideum with CA and NA as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 02:46:30 2007
Categories: Dictyostelium discoideum | Single protein | Almo, S.C. | Eichinger, L. | Fedorov, E.V. | Puius, Y.A. | Schleicher, M. | Sullivan, M. | CA | NA | Actin-binding protein | Calcium | Calcium-binding | Cytoskeleton | Gelsolin | Pip2 | Severin | Villin
