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==Crystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8A==
==Crystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8A==
<StructureSection load='3rtk' size='340' side='right' caption='[[3rtk]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3rtk' size='340' side='right'caption='[[3rtk]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3rtk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3rtk]] 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=3RTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RTK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL2, groEL-2, groEL2, hsp65, Rv0440, MT0456, MTV037.04 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3rtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rtk RCSB], [http://www.ebi.ac.uk/pdbsum/3rtk PDBsum]</span></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=3rtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtk OCA], [https://pdbe.org/3rtk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rtk RCSB], [https://www.ebi.ac.uk/pdbsum/3rtk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtk ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[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]
Mycobacterium tuberculosis expresses two proteins (Cpn60.1 and Cpn60.2) that belong to the chaperonin (Cpn) family of heat shock proteins. Studies have shown that the two proteins have different functional roles in the bacterial life cycle and that Cpn60.2 is essential for cell viability and may be involved in M. tuberculosis pathogenicity. Cpn60.2 does not form a tetradecameric double ring, which is typical of other Cpns. We have determined the crystal structure of recombinant Cpn60.2 to 2.8 A resolution by molecular replacement; the asymmetric unit (AU) contains a dimer, which is consistent with size-exclusion high-performance liquid chromatography and dynamic light-scattering measurements of the soluble recombinant protein. However, we suggest that the actual Cpn60.2 dimer may be different from that identified within the AU on the basis of surface contact stability, solvation free-energy gain, and functional aspects. Unlike the dimer found in the AU, which is formed through apical domain interactions, the dimeric form we propose here provides a free apical domain that is required for normal chaperone activity and may be involved in M. tuberculosis association with macrophages and arthrosclerosis plaque formation. Here we describe in detail the structural aspects that lead to Cpn60.2 dimer formation and prevent the formation of heptameric rings and tetradecameric double rings.
 
The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium tuberculosis at 2.8 A reveals possible modes of function.,Shahar A, Melamed-Frank M, Kashi Y, Shimon L, Adir N J Mol Biol. 2011 Sep 16;412(2):192-203. Epub 2011 Jul 23. PMID:21802426<ref>PMID:21802426</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chaperonin|Chaperonin]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Adir, N]]
[[Category: Adir N]]
[[Category: Kashi, Y]]
[[Category: Kashi Y]]
[[Category: Melamed-Frank, M]]
[[Category: Melamed-Frank M]]
[[Category: Shahar, A]]
[[Category: Shahar A]]
[[Category: Chaperone]]
[[Category: Chaperonin]]
[[Category: Heat shock protein]]

Latest revision as of 15:36, 14 March 2024

Crystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8ACrystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8A

Structural highlights

3rtk is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CH602_MYCTU Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[HAMAP-Rule:MF_00600]

See Also

3rtk, resolution 2.80Å

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