1vq0: Difference between revisions

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[[Image:1vq0.gif|left|200px]]<br /><applet load="1vq0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vq0, resolution 2.20&Aring;" />
'''Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution'''<br />


==About this Structure==
==Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution==
1VQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=UNL:'>UNL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQ0 OCA].  
<StructureSection load='1vq0' size='340' side='right'caption='[[1vq0]], [[Resolution|resolution]] 2.20&Aring;' 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]] 2.2&#8491;</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>


==Reference==
==See Also==
Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 A resolution., Jaroszewski L, Schwarzenbacher R, McMullan D, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA, Proteins. 2005 Nov 15;61(3):669-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16167343 16167343]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
[[Category: Single protein]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: CL]]
[[Category: EDO]]
[[Category: UNL]]
[[Category: ZN]]
[[Category: 33 kda chaperonin (heat shock protein 33 homolog) (hsp33)]]
[[Category: jcsg]]
[[Category: joint center for structural genomics]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomics]]
[[Category: tm1394]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:24 2008''

Latest revision as of 14:53, 20 September 2023

Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution

1vq0, resolution 2.20Å

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