5wyo

From Proteopedia

(Difference between revisions)

Revision as of 10:30, 14 June 2023

Solution structure of E.coli HdeA

Structural highlights

5wyo is a 2 chain structure with sequence from Escherichia coli O157:H7. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B, Chang Z. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem. 2005 Jul 22;280(29):27029-34. Epub 2005 May 23. PMID:15911614 doi:http://dx.doi.org/M503934200
↑ Kern R, Malki A, Abdallah J, Tagourti J, Richarme G. Escherichia coli HdeB is an acid stress chaperone. J Bacteriol. 2007 Jan;189(2):603-10. Epub 2006 Nov 3. PMID:17085547 doi:http://dx.doi.org/10.1128/JB.01522-06
↑ Malki A, Le HT, Milles S, Kern R, Caldas T, Abdallah J, Richarme G. Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. J Biol Chem. 2008 May 16;283(20):13679-87. Epub 2008 Mar 20. PMID:18359765 doi:http://dx.doi.org/M800869200
↑ Zhang M, Lin S, Song X, Liu J, Fu Y, Ge X, Fu X, Chang Z, Chen PR. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Nat Chem Biol. 2011 Sep 4;7(10):671-7. doi: 10.1038/nchembio.644. PMID:21892184 doi:http://dx.doi.org/10.1038/nchembio.644
↑ Yu XC, Yang C, Ding J, Niu X, Hu Y, Jin C. Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress. Biochemistry. 2017 Oct 31;56(43):5748-5757. doi: 10.1021/acs.biochem.7b00724., Epub 2017 Oct 17. PMID:29016106 doi:http://dx.doi.org/10.1021/acs.biochem.7b00724

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wyo"

Categories: Escherichia coli O157:H7 | Large Structures | Hu Y | Jin C | Yang C

@@ Line 1: / Line 1: @@
 ==Solution structure of E.coli HdeA==
-<StructureSection load='5wyo' size='340' side='right'caption='[[5wyo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='5wyo' size='340' side='right'caption='[[5wyo]]' 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://proteopedia.org/fgij/fg.htm?mol=5WYO FirstGlance]. <br>
+<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
+</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 ==
-[[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.
+[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 ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli O157:H7]]
 [[Category: Large Structures]]
-[[Category: Hu, Y]]
+[[Category: Hu Y]]
-[[Category: Jin, C]]
+[[Category: Jin C]]
-[[Category: Yang, C]]
+[[Category: Yang C]]
-[[Category: Chaperone]]
-[[Category: Periplasmic protein]]

5wyo

From Proteopedia

Revision as of 10:30, 14 June 2023

Solution structure of E.coli HdeA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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