3CXN

Structure of the Urease Accessory Protein UreF from Helicobacter pylori

Summary for 3CXN

• Entry DOI: 10.2210/pdb3cxn/pdb
• Descriptor: Urease accessory protein ureF, GLYCEROL (3 entities in total)
• Functional Keywords: helical, nickel, chaperone
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Cellular location: Cytoplasm : Q09065
• Total number of polymer chains: 3
• Total formula weight: 94109.19

Authors

Lam, R.,Johns, K.,Romanov, V.,Dong, A.,Wu-Brown, J.,Guthrie, J.,Dharamsi, A.,Thambipillai, D.,Mansoury, K.,Edwards, A.M.,Pai, E.F.,Chirgadze, N.Y. (deposition date: 2008-04-24, release date: 2009-05-12, Last modification date: 2024-10-09)

Primary citation

Lam, R.,Romanov, V.,Johns, K.,Battaile, K.P.,Wu-Brown, J.,Guthrie, J.L.,Hausinger, R.P.,Pai, E.F.,Chirgadze, N.Y.
Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.
Proteins, 78:2839-2848, 2010

PubMed 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.

PubMed: 20635345
DOI: 10.1002/prot.22802

Experimental method

X-RAY DIFFRACTION (1.55 Å)