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1bg8

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</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=1bg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bg8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bg8 PDBsum]</span></td></tr>
</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=1bg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bg8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bg8 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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>
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== References ==
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<references/>
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 07:40, 25 December 2014

HDEA FROM ESCHERICHIA COLI

1bg8, resolution 2.20Å

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