5zul: Difference between revisions
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<StructureSection load='5zul' size='340' side='right'caption='[[5zul]], [[Resolution|resolution]] 3.75Å' scene=''> | <StructureSection load='5zul' size='340' side='right'caption='[[5zul]], [[Resolution|resolution]] 3.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zul]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5zul]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZUL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zul OCA], [https://pdbe.org/5zul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zul RCSB], [https://www.ebi.ac.uk/pdbsum/5zul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zul ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B2HF11_MYCMM B2HF11_MYCMM] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5zul" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5zul" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium marinum M]] | ||
[[Category: Bhandari | [[Category: Bhandari S]] | ||
[[Category: Suguna | [[Category: Suguna K]] | ||
Latest revision as of 12:07, 22 November 2023
Small heat shock protein from Mycobacterium marinum M : Form-3Small heat shock protein from Mycobacterium marinum M : Form-3
Structural highlights
FunctionPublication Abstract from PubMedSmall heat shock proteins (sHSPs) are ATP-independent molecular chaperones present ubiquitously in all kingdoms of life. Their low molecular weight subunits associate to form higher order structures. Under conditions of stress, sHSPs prevent aggregation of substrate proteins by undergoing rapid changes in their conformation or stoichiometry. Polydispersity and dynamic nature of these proteins have made structural investigations through crystallography a daunting task. In pathogens like Mycobacteria, sHSPs are immuno-dominant antigens, enabling survival of the pathogen within the host and contributing to disease persistence. We characterized sHSPs from Mycobacterium marinum M and determined the crystal structure of one of these. The protein crystallized in three different conditions as dodecamers, with dimers arranged in a tetrahedral fashion to form a closed cage-like architecture. Interestingly, we found a pentapeptide bound to the dodecamers revealing one of the modes of sHSP-substrate interaction. Further, we have observed that ATP inhibits the chaperoning activity of the protein. Dodecameric structure of a small heat shock protein from Mycobacterium marinum M.,Bhandari S, Biswas S, Chaudhary A, Dutta S, Suguna K Proteins. 2019 Jan 11. doi: 10.1002/prot.25657. PMID:30632633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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