1svy
From Proteopedia
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|PDB= 1svy |SIZE=350|CAPTION= <scene name='initialview01'>1svy</scene>, resolution 1.75Å | |PDB= 1svy |SIZE=350|CAPTION= <scene name='initialview01'>1svy</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svy OCA], [http://www.ebi.ac.uk/pdbsum/1svy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svy RCSB]</span> | ||
}} | }} | ||
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[[Category: Schleicher, M.]] | [[Category: Schleicher, M.]] | ||
[[Category: Sullivan, M.]] | [[Category: Sullivan, M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NA]] | ||
[[Category: actin-binding protein]] | [[Category: actin-binding protein]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
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[[Category: villin]] | [[Category: villin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:40 2008'' |
Revision as of 20:47, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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