1sjp

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(New page: 200px<br /><applet load="1sjp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjp, resolution 3.20&Aring;" /> '''Mycobacterium tuberc...)
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[[Image:1sjp.gif|left|200px]]<br /><applet load="1sjp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sjp, resolution 3.20&Aring;" />
 
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'''Mycobacterium tuberculosis Chaperonin60.2'''<br />
 
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==Overview==
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==Mycobacterium tuberculosis Chaperonin60.2==
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Chaperonin 60s are a ubiquitous class of proteins that promote folding and, assembly of other cellular polypeptides in an ATP-dependent manner. The, oligomeric state of chaperonin 60s has been shown to be crucial to their, role as molecular chaperones. Chaperonin 60s are also known to be, important stimulators of the immune system. Mycobacterium tuberculosis, possesses a duplicate set of chaperonin 60s, both of which have been shown, to be potent cytokine stimulators. The M. tuberculosis chaperonin 60s are, present in the extracellular milieu at concentrations that are extremely, low for the formation of an oligomer. Here we present the crystal, structure of one of the chaperonin 60s of M. tuberculosis, also called, Hsp65 or chaperonin 60.2, at 3.2-A resolution. We were able to crystallize, the protein in its dimeric state. The unusual dimerization of the protein, leads to exposure of certain hydrophobic patches on the surface of the, protein, and we hypothesize that this might have relevance in binding to, immunogenic peptides, as it does in the eukaryotic homologs.
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<StructureSection load='1sjp' size='340' side='right'caption='[[1sjp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sjp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjp OCA], [https://pdbe.org/1sjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjp RCSB], [https://www.ebi.ac.uk/pdbsum/1sjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjp ProSAT], [https://www.topsan.org/Proteins/TBSGC/1sjp TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CH602_MYCTU CH602_MYCTU] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[HAMAP-Rule:MF_00600]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sj/1sjp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1sjp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP-dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones. Chaperonin 60s are also known to be important stimulators of the immune system. Mycobacterium tuberculosis possesses a duplicate set of chaperonin 60s, both of which have been shown to be potent cytokine stimulators. The M. tuberculosis chaperonin 60s are present in the extracellular milieu at concentrations that are extremely low for the formation of an oligomer. Here we present the crystal structure of one of the chaperonin 60s of M. tuberculosis, also called Hsp65 or chaperonin 60.2, at 3.2-A resolution. We were able to crystallize the protein in its dimeric state. The unusual dimerization of the protein leads to exposure of certain hydrophobic patches on the surface of the protein, and we hypothesize that this might have relevance in binding to immunogenic peptides, as it does in the eukaryotic homologs.
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==About this Structure==
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Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis.,Qamra R, Mande SC J Bacteriol. 2004 Dec;186(23):8105-13. PMID:15547284<ref>PMID:15547284</ref>
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1SJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJP OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis., Qamra R, Mande SC, J Bacteriol. 2004 Dec;186(23):8105-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15547284 15547284]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 1sjp" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Mande, S.C.]]
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[[Category: Qamra, R.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: chaperone]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:25:38 2007''
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==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Mande SC]]
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[[Category: Qamra R]]

Current revision

Mycobacterium tuberculosis Chaperonin60.2

PDB ID 1sjp

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