Caly, DL,O'Toole, PW,Moore, SA;

2010

January

Rna-A Publication of The Rna Society

The 2.2-angstrom Structure of the HP0958 Protein from Helicobacter pylori Reveals a Kinked Anti-Parallel Coiled-Coil Hairpin Domain and a Highly Conserved Zn-Ribbon Domain

Validated

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flagellum biogenesis mRNA chaperone Zn ribbon coiled-coil hairpin Helicobacter pylori RNA INTERACTIONS CAULOBACTER-CRESCENTUS GNOTOBIOTIC PIGLETS FLAGELLIN SYNTHESIS MOLECULAR GRAPHICS COMPLEX GENE RECOGNITION REGULATOR MOTILITY

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We have determined the 2.2-angstrom 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 (sigma(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. (C) 2010 Elsevier Ltd. All rights reserved.

DOI 10.1016/j.jmb.2010.08.051