title: Structure of Vibrio cholerae ribosome hibernation promoting factor.
abstract: The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0 Å resolution. The crystal was phased by two-wavelength MAD using cocrystallized cobalt. The asymmetric unit contained two molecules of HPF linked by four Co atoms. The metal-binding sites observed in the crystal are probably not related to biological function. The structure of HPF has a typical β-α-β-β-β-α fold consistent with previous structures of YfiA and HPF from Escherichia coli. Comparison of the new structure with that of HPF from E. coli bound to the Thermus thermophilus ribosome [Polikanov et al. (2012), Science, 336, 915-918] shows that no significant structural changes are induced in HPF by binding.
authors.affiliation: Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 E. Adams Avenue, Syracuse, NY 13210, USA.
authors.forename: Heather
authors.initials: H
authors.lastname: De Bari
authors.forename: Edward A
authors.initials: EA
authors.lastname: Berry
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003035:Cobalt / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000737:chemistry / Q000378:metabolism; D014734:Vibrio cholerae / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; C422854:HPF protein, E coli; D012269:Ribosomal Proteins; D003035:Cobalt
keywords: MAD; Vibrio cholerae; cobalt; cold shock; hibernation promotion factor; metal-binding site; ribosome hibernation; ribosome-binding proteins; stationary phase