title: Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.
abstract: Urease plays a central role in the pathogenesis of Helicobacter pylori in humans. Maturation of this nickel metalloenzyme in bacteria requires the participation of the accessory proteins UreD (termed UreH in H. pylori), UreF, and UreG, which form sequential complexes with the urease apoprotein as well as UreE, a metallochaperone. Here, we describe the crystal structure of C-terminal truncated UreF from H. pylori (residues 1-233), the first UreF structure to be determined, at 1.55 A resolution using SAD methods. UreF forms a dimer in vitro and adopts an all-helical fold congruent with secondary structure prediction. On the basis of evolutionary conservation analysis, the structure reveals a probable binding surface for interaction with other urease components as well as key conserved residues of potential functional relevance.
authors.affiliation: Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, Toronto, Ontario M5G 2C4, Canada.
authors.forename: Robert
authors.initials: R
authors.lastname: Lam
authors.forename: Vladimir
authors.initials: V
authors.lastname: Romanov
authors.forename: Kathy
authors.initials: K
authors.lastname: Johns
authors.forename: Kevin P
authors.initials: KP
authors.lastname: Battaile
authors.forename: Jean
authors.initials: J
authors.lastname: Wu-Brown
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Guthrie
authors.forename: Robert P
authors.initials: RP
authors.lastname: Hausinger
authors.forename: Emil F
authors.initials: EF
authors.lastname: Pai
authors.forename: Nickolay Y
authors.initials: NY
authors.lastname: Chirgadze
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D014510:Urease / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; C101639:UreF protein, bacteria; D014510:Urease