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1dj8
From Proteopedia
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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=1dj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dj8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dj8 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=1dj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dj8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dj8 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:28, 25 December 2014
CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA
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