Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori

• Published in: Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2010-10, Vol.78 (13), p.2839-2848
• Main Authors: Lam, Robert, Romanov, Vladimir, Johns, Kathy, Battaile, Kevin P., Wu-Brown, Jean, Guthrie, Jennifer L., Hausinger, Robert P., Pai, Emil F., Chirgadze, Nickolay Y.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Binding Sites - genetics; ConSurf; Crystallography, X-Ray; dimer; Helicobacter pylori - enzymology; Helicobacter pylori - genetics; Models, Molecular; Molecular Sequence Data; Mutation; Protein Folding; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Secondary; protein-protein interactions; sequence conservation; Sequence Homology, Amino Acid; urease; Urease - chemistry; Urease - genetics
• ISSN: 0887-3585; 1097-0134
• DOI: 10.1002/prot.22802

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 Å 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. Proteins 2010. © 2010 Wiley‐Liss, Inc.