3sf5

Crystal Structure of Helicobacter pylori Urease Accessory Protein UreF/H complex

spinqualitylabelsall models 3sf5, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sf5 is a 4 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.495Å Ligands: GOL, PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UREF_HELPY Required for maturation of urease via the functional incorporation of the urease nickel metallocenter (By similarity).[HAMAP-Rule:MF_01385] Publication Abstract from PubMed Colonization of Helicobacter pylori in the acidic environment of the human stomach depends on the neutralizing activity of urease. Activation of apo-urease involves carboxylation of lysine 219 and insertion of two nickel ions. In H. pylori, this maturation process involves four urease accessory proteins as follows: UreE, UreF, UreG, and UreH. It is postulated that the apo-urease interacts with UreF, UreG, and UreH to form a pre-activation complex that undergoes GTP-dependent activation of urease. The crystal structure of the UreF-UreH complex reveals conformational changes in two distinct regions of UreF upon complex formation. First, the flexible C-terminal residues of UreF become ordered, forming an extra helix alpha10 and a loop structure stabilized by hydrogen bonds involving Arg-250. Second, the first turn of helix alpha2 uncoils to expose a conserved residue, Tyr-48. Substitution of R250A or Y48A in UreF abolishes the formation of the heterotrimeric complex of UreG-UreF-UreH and abolishes urease maturation. Our results suggest that the C-terminal residues and helix alpha2 of UreF are essential for the recruitment of UreG for the formation of the pre-activation complex. The molecular mass of the UreF-UreH complex determined by static light scattering was 116 +/- 2.3 kDa, which is consistent with the quaternary structure of a dimer of heterodimers observed in the crystal structure. Taking advantage of the unique 2-fold symmetry observed in both the crystal structures of H. pylori urease and the UreF-UreH complex, we proposed a topology model of the pre-activation complex for urease maturation. Assembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEX.,Fong YH, Wong HC, Chuck CP, Chen YW, Sun H, Wong KB J Biol Chem. 2011 Dec 16;286(50):43241-9. Epub 2011 Oct 19. PMID:22013070 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urease accessory protein

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