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6bie

From Proteopedia

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m (Protected "6bie" [edit=sysop:move=sysop])
Current revision (14:41, 4 October 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6bie is ON HOLD
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==MISREADING CHAPERONE-SUBSTRATE COMPLEXES FROM RANDOM NOISE==
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<StructureSection load='6bie' size='340' side='right'caption='[[6bie]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6bie]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BIE 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">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=6bie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bie OCA], [https://pdbe.org/6bie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bie RCSB], [https://www.ebi.ac.uk/pdbsum/6bie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bie ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPY_ECOLI SPY_ECOLI] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref> <ref>PMID:24497545</ref> <ref>PMID:26619265</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 K-12]]
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[[Category: Large Structures]]
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[[Category: WANG J]]

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MISREADING CHAPERONE-SUBSTRATE COMPLEXES FROM RANDOM NOISE

PDB ID 6bie

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