3cxn

Structure of the Urease Accessory Protein UreF from Helicobacter pylori

spinqualitylabelsall models 3cxn, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cxn is a 3 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL NonStd Res: MSE Gene: ureF (Helicobacter pylori) Resources: FirstGlance, OCA, RCSB, PDBsum Function [UREF_HELPY] Required for maturation of urease via the functional incorporation of the urease nickel metallocenter (By similarity).[HAMAP-Rule:MF_01385] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Proteins 2010. (c) 2010 Wiley-Liss, Inc. Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.,Lam R, Romanov V, Johns K, Battaile KP, Wu-Brown J, Guthrie JL, Hausinger RP, Pai EF, Chirgadze NY Proteins. 2010 Jun 14. PMID:20635345 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urease accessory protein

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