1svy: Difference between revisions

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-[[Image:1svy.gif|left|200px]]
- {{Structure
+==SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE==
-|PDB= 1svy |SIZE=350|CAPTION= <scene name='initialview01'>1svy</scene>, resolution 1.75&Aring;
+<StructureSection load='1svy' size='340' side='right'caption='[[1svy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
+<table><tr><td colspan='2'>[[1svy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1SVY FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svy OCA], [https://pdbe.org/1svy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svy RCSB], [https://www.ebi.ac.uk/pdbsum/1svy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svy_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svy ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-'''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''
+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>
+</div>
+<div class="pdbe-citations 1svy" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Severin|Severin]]
+== References ==
-==About this Structure==
+<references/>
-SVY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVY OCA].
+__TOC__
+</StructureSection>
-==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:[http://www.ncbi.nlm.nih.gov/pubmed/10820002 10820002]
 [[Category: Dictyostelium discoideum]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Almo, S C.]]
+[[Category: Almo SC]]
-[[Category: Eichinger, L.]]
+[[Category: Eichinger L]]
-[[Category: Fedorov, E V.]]
+[[Category: Fedorov EV]]
-[[Category: Puius, Y A.]]
+[[Category: Puius YA]]
-[[Category: Schleicher, M.]]
+[[Category: Schleicher M]]
-[[Category: Sullivan, M.]]
+[[Category: Sullivan M]]
-[[Category: CA]]
-[[Category: NA]]
-[[Category: actin-binding protein]]
-[[Category: calcium]]
-[[Category: calcium-binding]]
-[[Category: cytoskeleton]]
-[[Category: gelsolin]]
-[[Category: pip2]]
-[[Category: severin]]
-[[Category: villin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:21 2008''