7ywy

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'''Unreleased structure'''
 
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The entry 7ywy is ON HOLD until Paper Publication
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==Structure of the GroEL chaperonin in complex with the CnoX chaperedoxin==
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<StructureSection load='7ywy' size='340' side='right'caption='[[7ywy]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7ywy]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YWY FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=7ywy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ywy OCA], [https://pdbe.org/7ywy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ywy RCSB], [https://www.ebi.ac.uk/pdbsum/7ywy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ywy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CNOX_ECOLI CNOX_ECOLI] Chaperedoxin that combines a chaperone activity with a redox-protective function (PubMed:16563353, PubMed:18657513, PubMed:29754824). Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation (PubMed:29754824). Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes (PubMed:29754824). After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases (PubMed:29754824). Lacks oxidoreductase activity (PubMed:21498507, PubMed:29754824).<ref>PMID:16563353</ref> <ref>PMID:18657513</ref> <ref>PMID:21498507</ref> <ref>PMID:29754824</ref>
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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: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Collet JF]]
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[[Category: Dupuy E]]
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[[Category: Remaut H]]
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[[Category: Van der Verren SE]]

Current revision

Structure of the GroEL chaperonin in complex with the CnoX chaperedoxin

PDB ID 7ywy

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