Structural highlights
Function
PYRE_STRMU Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
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
Orotate phosphoribosyltransferase (OPRTase) catalyzes the OMP-forming step in de novo pyrimidine-nucleotide biosynthesis. Here, the crystal structure of OPRTase from the caries pathogen Streptococcus mutans is reported at 2.4 A resolution. S. mutans OPRTase forms a symmetric dimer and each monomer binds two sulfates at the active sites. The structural symmetry of the sulfate-binding sites and the missing loops in this structure are consistent with a symmetric catalysis mechanism.
Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.,Liu CP, Xu R, Gao ZQ, Xu JH, Hou HF, Li LQ, She Z, Li LF, Su XD, Liu P, Dong YH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt, 5):498-502. Epub 2010 Apr 29. PMID:20445243[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu CP, Xu R, Gao ZQ, Xu JH, Hou HF, Li LQ, She Z, Li LF, Su XD, Liu P, Dong YH. Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt, 5):498-502. Epub 2010 Apr 29. PMID:20445243 doi:10.1107/S1744309110009243
