1dj8
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1dj8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dj8 RCSB]</span> | ||
}} | }} | ||
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[[Category: alpha helical]] | [[Category: alpha helical]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:42 2008'' |
Revision as of 16:42, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA
Overview
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.
About this Structure
1DJ8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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