6owz: Difference between revisions

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New page: '''Unreleased structure''' The entry 6owz is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6owz is ON HOLD
==Spy H96L:Im7 L19pI-Phe complex; multiple anomalous datasets contained herein for element identification==
 
<StructureSection load='6owz' size='340' side='right'caption='[[6owz]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6owz]] 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=6OWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OWZ FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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=6owz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owz OCA], [https://pdbe.org/6owz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6owz RCSB], [https://www.ebi.ac.uk/pdbsum/6owz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6owz 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]]

Latest revision as of 07:18, 11 October 2023

Spy H96L:Im7 L19pI-Phe complex; multiple anomalous datasets contained herein for element identification

6owz, resolution 2.05Å

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