1dj8
From Proteopedia
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| - | [[Image:1dj8.jpg|left|200px]] | ||
| - | + | ==CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA== | |
| - | + | <StructureSection load='1dj8' size='340' side='right'caption='[[1dj8]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJ8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1dj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj8 OCA], [https://pdbe.org/1dj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dj8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dj8 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | ''' | + | == Publication Abstract from PubMed == |
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The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 A resolution. The single domain alpha-helical protein is found in the periplasmic space, where it supports an acid resistance phenotype essential for infectivity of enteric bacterial pathogens, such as Shigella and E. coli. Functional studies demonstrate that HDEA is activated by a dimer-to-monomer transition at acidic pH, leading to suppression of aggregation by acid-denatured proteins. We suggest that HDEA may support chaperone-like functions during the extremely acidic conditions. | The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 A resolution. The single domain alpha-helical protein is found in the periplasmic space, where it supports an acid resistance phenotype essential for infectivity of enteric bacterial pathogens, such as Shigella and E. coli. Functional studies demonstrate that HDEA is activated by a dimer-to-monomer transition at acidic pH, leading to suppression of aggregation by acid-denatured proteins. We suggest that HDEA may support chaperone-like functions during the extremely acidic conditions. | ||
| - | + | HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria.,Gajiwala KS, Burley SK J Mol Biol. 2000 Jan 21;295(3):605-12. PMID:10623550<ref>PMID:10623550</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1dj8" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | [[Category: Burley | + | <references/> |
| - | [[Category: Gajiwala | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Burley SK]] | ||
| + | [[Category: Gajiwala KS]] | ||
Current revision
CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA
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