3dez
From Proteopedia
Jump to navigationJump to search
Crystal structure of Orotate phosphoribosyltransferase from Streptococcus mutans
| ||||||||||||
Structural highlights
FunctionPYRE_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 PubMedOrotate 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 AlsoReferences
| ||||||||||||||||||||
This page was last modified 15:08, 1 November 2023.