View source for 3m6c


==Crystal structure of Mycobacterium tuberculosis GroEL1 apical domain==
<StructureSection load='3m6c' size='340' side='right'caption='[[3m6c]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3m6c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M6C 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6c OCA], [https://pdbe.org/3m6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m6c RCSB], [https://www.ebi.ac.uk/pdbsum/3m6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CH601_MYCTU CH601_MYCTU] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.<ref>PMID:21094166</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GroEL is a group I chaperonin that facilitates protein folding and prevents protein aggregation in the bacterial cytosol. Mycobacteria are unusual in encoding two or more copies of GroEL in their genome. While GroEL2 is essential for viability and likely functions as the general housekeeping chaperonin, GroEL1 is dispensable, but its structure and function remain unclear. Here, we present the 2.2-A-resolution crystal structure of a 23-kDa fragment of Mycobacterium tuberculosis GroEL1 consisting of an extended apical domain. Our X-ray structure of the GroEL1 apical domain closely resembles those of Escherichia coli GroEL and M. tuberculosis GroEL2, thus highlighting the remarkable structural conservation of bacterial chaperonins. Notably, in our structure, the proposed substrate-binding site of GroEL1 interacts with the N-terminal region of a symmetry-related neighboring GroEL1 molecule. The latter is consistent with the known GroEL apical domain function in substrate binding and is supported by results obtained from using peptide array technology. Taken together, these data show that the apical domains of M. tuberculosis GroEL paralogs are conserved in three-dimensional structure, suggesting that GroEL1, like GroEL2, is a chaperonin.

Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a Chaperonin.,Sielaff B, Lee KS, Tsai FT J Mol Biol. 2010 Nov 19. PMID:21094166<ref>PMID:21094166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3m6c" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Lee K]]
[[Category: Sielaff B]]
[[Category: Tsai FTF]]