View source for 3mii


==Crystal structure of Y0R391Cp/HSP33 from Saccharomyces cerevisiae==
<StructureSection load='3mii' size='340' side='right'caption='[[3mii]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mii]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MII 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3mii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mii OCA], [https://pdbe.org/3mii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mii RCSB], [https://www.ebi.ac.uk/pdbsum/3mii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mii ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSP33_YEAST HSP33_YEAST] Probable protease. May act as a chaperone (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Saccharomyces cerevisiae Hsp33/YOR391Cp is a member of the ThiI/DJ-1/PfpI superfamily. Hsp33 was overexpressed in Escherichia coli and its crystal structure was determined at 2.40 A resolution. Structural comparison revealed that Hsp33 adopts an alpha/beta-hydrolase fold and possesses the putative Cys-His-Glu catalytic triad common to the Hsp31 family, suggesting that Hsp33 and Hsp31 share similar aminopeptidase activity, while structural deviations in helices alpha2-alpha3 of the core domain might be responsible for the access of different peptide substrates.

Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.,Guo PC, Zhou YY, Ma XX, Li WF Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1557-61. Epub 2010 Nov 16. PMID:21139195<ref>PMID:21139195</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mii" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Guo P-C]]
[[Category: Li W-F]]
[[Category: Zhou C-Z]]
[[Category: Zhou Y-Y]]