1svy

<StructureSection load='1svy' size='340' side='right' caption='[[1svy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1svy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SVY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1svy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1svy RCSB], [http://www.ebi.ac.uk/pdbsum/1svy PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/SEVE_DICDI SEVE_DICDI]] Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svy_consurf.spt"</scriptWhenChecked>

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== 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<ref>PMID:10820002</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1svy" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 11735]]

[[Category: Almo, S C]]

[[Category: Eichinger, L]]

[[Category: Fedorov, E V]]

[[Category: Puius, Y A]]

[[Category: Schleicher, M]]

[[Category: Sullivan, M]]

[[Category: Villin]]