6owy
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Spy H96L:Im7 K20pI-Phe complex; multiple anomalous datasets contained herein for element identification== | |
- | + | <StructureSection load='6owy' size='340' side='right'caption='[[6owy]], [[Resolution|resolution]] 2.07Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6owy]] is a 2 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=6OWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OWY 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]] 2.07Å</td></tr> | |
- | [[Category: | + | <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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6owy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owy OCA], [https://pdbe.org/6owy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6owy RCSB], [https://www.ebi.ac.uk/pdbsum/6owy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6owy ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia coli]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Bardwell JCA]] | ||
+ | [[Category: Duman R]] | ||
+ | [[Category: El Omari K]] | ||
+ | [[Category: Horowitz S]] | ||
+ | [[Category: Mykhaylyk V]] | ||
+ | [[Category: Rocchio S]] | ||
+ | [[Category: Wagner A]] | ||
+ | [[Category: Yan Z]] |
Current revision
Spy H96L:Im7 K20pI-Phe complex; multiple anomalous datasets contained herein for element identification
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Categories: Escherichia coli | Large Structures | Bardwell JCA | Duman R | El Omari K | Horowitz S | Mykhaylyk V | Rocchio S | Wagner A | Yan Z