5wyo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of E.coli HdeA== | |
| + | <StructureSection load='5wyo' size='340' side='right'caption='[[5wyo]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wyo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WYO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=5wyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wyo OCA], [https://pdbe.org/5wyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wyo RCSB], [https://www.ebi.ac.uk/pdbsum/5wyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wyo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HDEA_ECOLI HDEA_ECOLI] Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.<ref>PMID:15911614</ref> <ref>PMID:17085547</ref> <ref>PMID:18359765</ref> <ref>PMID:21892184</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bacterial acid-resistant chaperone HdeA is a "conditionally disordered" protein that functions at low pH when it undergoes a transition from a well-folded dimer to an unfolded monomer. The dimer dissociation and unfolding processes result in exposure of hydrophobic surfaces that allows binding to a broad range of client proteins. To fully elucidate the chaperone mechanism of HdeA, it is crucial to understand how the activated HdeA interacts with its native substrates during acid stress. Herein, we present a nuclear magnetic resonance study of the pH-dependent HdeA-substrate interactions. Our results show that the activation of HdeA is not only induced by acidification but also regulated by the presence of unfolded substrates. The variable extent of unfolding of substrates differentially regulates the HdeA-substrate interaction, and the binding further affects the HdeA conformation. Finally, we show that HdeA binds its substrates heterogeneously, and the "amphiphilic" model for HdeA-substrate interaction is discussed. | ||
| - | + | Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress.,Yu XC, Yang C, Ding J, Niu X, Hu Y, Jin C Biochemistry. 2017 Oct 31;56(43):5748-5757. doi: 10.1021/acs.biochem.7b00724., Epub 2017 Oct 17. PMID:29016106<ref>PMID:29016106</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5wyo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hu | + | == References == |
| - | [[Category: Yang | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli O157:H7]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hu Y]] | ||
| + | [[Category: Jin C]] | ||
| + | [[Category: Yang C]] | ||
Current revision
Solution structure of E.coli HdeA
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