Ontology highlight
ABSTRACT:
SUBMITTER: Lam R
PROVIDER: S-EPMC2978904 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Lam Robert R Romanov Vladimir V Johns Kathy K Battaile Kevin P KP Wu-Brown Jean J Guthrie Jennifer L JL Hausinger Robert P RP Pai Emil F EF Chirgadze Nickolay Y NY
Proteins 20101001 13
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 us ...[more]