TY  - JOUR
  - 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
  - ()
  - 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
  - 403
  - 405
  - 419
  - 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
DA  - 2010/01
ER  - 

@article{V70046560,
   = {Caly,  DL and O'Toole,  PW and 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},
   = {()},
   = {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},
   = {403},
  pages = {405--419},
   = {{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},
  source = {IRIS}
}