title: ¹³C, ¹⁵N and ¹H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6.
abstract: HdeA is a small chaperone found in the periplasm of several common pathogenic bacteria (Escherichia coli, Shigella flexneri and Brucella abortus) which are the leading causes of dysentery worldwide, especially in developing countries. Its job is to protect other periplasmic proteins from aggregating as the bacteria pass through the low pH environment of the human stomach on their way to infect the intestines. HdeA is an inactive folded dimer at neutral pH, but becomes a disordered active monomer at pH < 3. To initiate NMR characterization of HdeA at pH 6, 94% of the backbone and 86% of the side chain chemical shifts have been assigned. The loop linking helices B and C remains largely unassigned due to missing peaks in the (1)H-(15)N HSQC and other spectra, most likely due to intermediate timescale chemical exchange. Many of the weakest intensity backbone peaks correspond to residues that surround this loop within the tertiary structure. Assignment experiments have therefore helped to provide preliminary clues about the region of the protein that may be most responsible for initiating unfolding as the pH drops, and constitute an important first step in improving our understanding of, and ultimately combatting, HdeA activity.
authors.affiliation: Department of Chemistry and Biochemistry, California State University Northridge, 18111 Nordhoff St., Northridge, CA, 91330-8262, USA, karin.crowhurst@csun.edu.
authors.forename: K A
authors.initials: KA
authors.lastname: Crowhurst
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C084501:hdeA protein, E coli