3SF5
Crystal Structure of Helicobacter pylori Urease Accessory Protein UreF/H complex
Summary for 3SF5
| Entry DOI | 10.2210/pdb3sf5/pdb |
| Related | 2WGL 3O1Q |
| Descriptor | Urease accessory protein ureF, Urease accessory protein ureH, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | urease accessory protein, uref, ureh, chaperone |
| Biological source | Helicobacter pylori More |
| Cellular location | Cytoplasm (By similarity): Q09065 Q09067 |
| Total number of polymer chains | 4 |
| Total formula weight | 118437.52 |
| Authors | Fong, Y.H.,Chen, Y.W.,Wong, K.B. (deposition date: 2011-06-12, release date: 2011-11-02, Last modification date: 2023-11-01) |
| 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 Cited by 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: 22013070DOI: 10.1074/jbc.M111.296830 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.495 Å) |
Structure validation
Download full validation report
