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| | ==Solution structure of a bacterial chaperone== | | ==Solution structure of a bacterial chaperone== |
| - | <StructureSection load='2myj' size='340' side='right' caption='[[2myj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2myj' size='340' side='right'caption='[[2myj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2myj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2myj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hdeB, yhhD, yhiC, b3509, JW5669 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hdeB, yhhD, yhiC, b3509, JW5669 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2myj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myj OCA], [http://pdbe.org/2myj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myj RCSB], [http://www.ebi.ac.uk/pdbsum/2myj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2myj ProSAT]</span></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=2myj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myj OCA], [https://pdbe.org/2myj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myj RCSB], [https://www.ebi.ac.uk/pdbsum/2myj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HDEB_ECOLI HDEB_ECOLI]] Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.<ref>PMID:17085547</ref> | + | [[https://www.uniprot.org/uniprot/HDEB_ECOLI HDEB_ECOLI]] Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.<ref>PMID:17085547</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ding, J]] | | [[Category: Ding, J]] |
| | [[Category: Hu, Y]] | | [[Category: Hu, Y]] |
| | [[Category: Jin, C]] | | [[Category: Jin, C]] |
| | [[Category: Chaperone]] | | [[Category: Chaperone]] |
| Structural highlights
Function
[HDEB_ECOLI] Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.[1]
Publication Abstract from PubMed
Enteric bacteria encounter extreme acidity when passing through hosts' stomach. Since the bacterial periplasmic space quickly equilibrates with outer environment, an efficient acid resistance mechanism is essential in preventing irreversible protein denaturation/aggregation and maintaining bacteria viability. HdeB, along with its homolog HdeA, was identified as a periplasmic acid-resistant chaperone. Both proteins exist as homodimers and share similar monomeric structures under neutral pH, while showing different dimeric packing interfaces. Previous investigations show that HdeA functions through an acid-induced dimer-to-monomer transition and partial unfolding at low pH (pH 2-3), resulting in exposure of hydrophobic surfaces that bind substrate proteins. In contrast, HdeB appears to have a much higher optimal activation pH (pH 4-5), under which condition the protein maintains a well-folded dimer and the mechanism for its chaperone activity remains elusive. Herein, we present an NMR study of HdeB to investigate its dynamic properties. Our results reveal that HdeB undergoes significant micro- to milli-second timescale conformational exchanges at neutral to near-neutral pH, under the later condition it exhibits optimal activity. The current study indicates that HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA.
HdeB chaperone activity is coupled to its intrinsic dynamic properties.,Ding J, Yang C, Niu X, Hu Y, Jin C Sci Rep. 2015 Nov 23;5:16856. doi: 10.1038/srep16856. PMID:26593705[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ Ding J, Yang C, Niu X, Hu Y, Jin C. HdeB chaperone activity is coupled to its intrinsic dynamic properties. Sci Rep. 2015 Nov 23;5:16856. doi: 10.1038/srep16856. PMID:26593705 doi:http://dx.doi.org/10.1038/srep16856
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