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1vq0
From Proteopedia
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| - | [[Image:1vq0.gif|left|200px]] | ||
| - | < | + | ==Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution== |
| - | + | <StructureSection load='1vq0' size='340' side='right'caption='[[1vq0]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1vq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQ0 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1vq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vq0 OCA], [https://pdbe.org/1vq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vq0 RCSB], [https://www.ebi.ac.uk/pdbsum/1vq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vq0 ProSAT], [https://www.topsan.org/Proteins/JCSG/1vq0 TOPSAN]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HSLO_THEMA HSLO_THEMA] Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (By similarity). | ||
| + | == 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/vq/1vq0_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=1vq0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | [[Category: | + | |
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
| - | [[Category: Jcsg]] | ||
| - | [[Category: Joint center for structural genomic]] | ||
| - | [[Category: Protein structure initiative]] | ||
| - | [[Category: Psi]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Tm1394]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:46:56 2008'' | ||
Current revision
Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution
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