3NA7

2.2 Angstrom Structure of the HP0958 Protein from Helicobacter pylori CCUG 17874

Summary for 3NA7

• Entry DOI: 10.2210/pdb3na7/pdb
• Descriptor: HP0958, ZINC ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: flagellar biogenesis, flagellum export, c4 zn-ribbon, coiled-coil, post-transcriptional, gene regulation, chaperone
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Total number of polymer chains: 1
• Total formula weight: 30127.04

Authors

Caly, D.L.,O'Toole, P.W.,Moore, S.A. (deposition date: 2010-06-01, release date: 2010-09-22, Last modification date: 2024-03-20)

Primary citation

Caly, D.L.,O'Toole, P.W.,Moore, S.A.
The 2.2-A Structure of the HP0958 Protein from Helicobacter pylori Reveals a Kinked Anti-Parallel Coiled-Coil Hairpin Domain and a Highly Conserved Zn-Ribbon Domain
J.Mol.Biol., 403:405-419, 2010

PubMed Abstract: We have determined the 2.2-Å structure of the HP0958 protein from the human gastric pathogen Helicobacter pylori. HP0958 is essential for flagellum formation and motility. It functions as a chaperone for RpoN (σ(54)) and also controls the stability and translation of mRNA for the major flagellin subunit FlaA. The protein is composed of a highly elongated and kinked coiled-coil hairpin domain (residues 1-170), followed by a C(4) Zn-ribbon domain (residues 174-238). The Zn-ribbon domain is rich in aromatic and positively charged amino acid residues. Electrophoretic mobility shift assays identified residues in a positively charged region of the Zn-ribbon domain of HP0958 whose mutation alters the mobility of an HP0958-flaA mRNA complex. Mutation of surface residues in the coiled-coil domain did not result in an observable change in the mobility of the HP0958-flaA transcript complex. The data thus suggest the arrangement of HP0958 into distinct structural and functional domains.

PubMed: 20826163
DOI: 10.1016/j.jmb.2010.08.051

Experimental method

X-RAY DIFFRACTION (2.2 Å)