Urease accessory protein

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models Structure of UreE complex with formate and Ni+2 (PDB code 3tj8) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Urease accessory protein (Ure) is a Ni-containing urea hydrolase involved in nitrogen recycling from arginine, ureide and purines. Ure proteins are involved in urease activation by the transfer of Ni into the protein[1]. UreE - see Molecular Playground/UreE. UreF - modulates the activation process of urease by eliminating the binding of Ni irons to noncarbamylated protein[2]. UreG - modulates the activation process of urease in plants [3]. UreH - forms in combination with UreF and UreG a pre-activation complex which activates urease[4]. UreI - probably facilitates nickel incorporation. Structural highlights The [5]. Water molecule is shown as red sphere.

3D structures of urease accessory protein

Updated on 13-March-2024

References

1. ↑ Witte CP, Isidore E, Tiller SA, Davies HV, Taylor MA. Functional characterisation of urease accessory protein G (ureG) from potato. Plant Mol Biol. 2001 Jan;45(2):169-79. PMID:11289508
2. ↑ Moncrief MB, Hausinger RP. Purification and activation properties of UreD-UreF-urease apoprotein complexes. J Bacteriol. 1996 Sep;178(18):5417-21. PMID:8808930
3. ↑ Myrach T, Zhu A, Witte CP. The assembly of the plant urease activation complex and the essential role of the urease accessory protein G (UreG) in delivery of nickel to urease. J Biol Chem. 2017 Sep 1;292(35):14556-14565. doi: 10.1074/jbc.M117.780403. Epub, 2017 Jul 14. PMID:28710280 doi:http://dx.doi.org/10.1074/jbc.M117.780403
4. ↑ Fong YH, Wong HC, Chuck CP, Chen YW, Sun H, Wong KB. Assembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEX. J Biol Chem. 2011 Dec 16;286(50):43241-9. Epub 2011 Oct 19. PMID:22013070 doi:10.1074/jbc.M111.296830
5. ↑ Banaszak K, Martin-Diaconescu V, Bellucci M, Zambelli B, Rypniewski W, Maroney MJ, Ciurli S. Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveal a role for the disordered C-terminal arm in metal trafficking. Biochem J. 2011 Oct 20. PMID:22010876 doi:10.1042/BJ20111659