1DJ8

CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA

Summary for 1DJ8

Entry DOI	10.2210/pdb1dj8/pdb
Descriptor	PROTEIN HNS-DEPENDENT EXPRESSION A (2 entities in total)
Functional Keywords	alpha helical, structural protein
Biological source	Escherichia coli
Total number of polymer chains	6
Total formula weight	58517.29
Authors	Gajiwala, K.S.,Burley, S.K. (deposition date: 1999-12-02, release date: 1999-12-10, Last modification date: 2024-10-30)
Primary citation	Gajiwala, K.S.,Burley, S.K. HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. J.Mol.Biol., 295:605-612, 2000 Cited by PubMed Abstract: 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. PubMed: 10623550 DOI: 10.1006/jmbi.1999.3347 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation