5wyo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of E.coli HdeA== | |
| + | <StructureSection load='5wyo' size='340' side='right' caption='[[5wyo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wyo]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WYO FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wyo OCA], [http://pdbe.org/5wyo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wyo RCSB], [http://www.ebi.ac.uk/pdbsum/5wyo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wyo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HDEA_ECO57 HDEA_ECO57]] Required for optimal acid stress protection. Exhibits a chaperone-like activity only at low pH by suppressing non-specifically the aggregation of denaturated periplasmic proteins. | ||
| + | <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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5wyo" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hu, Y]] | [[Category: Hu, Y]] | ||
| + | [[Category: Jin, C]] | ||
[[Category: Yang, C]] | [[Category: Yang, C]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Periplasmic protein]] | ||
Revision as of 07:45, 22 November 2017
Solution structure of E.coli HdeA
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Categories: Hu, Y | Jin, C | Yang, C | Chaperone | Periplasmic protein
