3O1Q

Native Crystal Structure of Helicobacter pylori Urease Accessory Protein UreF

Summary for 3O1Q

• Entry DOI: 10.2210/pdb3o1q/pdb
• Related: 2wgl
• Descriptor: Urease accessory protein ureF (2 entities in total)
• Functional Keywords: urease maturation, metal binding protein
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Cellular location: Cytoplasm (By similarity): Q09065
• Total number of polymer chains: 3
• Total formula weight: 85955.50

Authors

Fong, Y.H.,Chen, Y.W.,Wong, K.B. (deposition date: 2010-07-21, release date: 2010-08-18, Last modification date: 2024-02-21)

Primary citation

Fong, Y.H.,Wong, H.C.,Chuck, C.P.,Chen, Y.W.,Sun, H.,Wong, K.B.
Assembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEX.
J.Biol.Chem., 286:43241-43249, 2011

PubMed Abstract: 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 α10 and a loop structure stabilized by hydrogen bonds involving Arg-250. Second, the first turn of helix α2 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 α2 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.

PubMed: 22013070
DOI: 10.1074/jbc.M111.296830

Experimental method

X-RAY DIFFRACTION (1.85 Å)