Open AccessStructure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans
Author(s) -
Liu ChaoPei,
Xu Rui,
Gao ZengQiang,
Xu JianHua,
Hou HaiFeng,
Li LiQin,
She Zhun,
Li LanFen,
Su XiaoDong,
Liu Peng,
Dong YuHui
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110009243
Subject(s) - streptococcus mutans , chemistry , dimer , phosphoribosyltransferase , nucleotide , monomer , biochemistry , stereochemistry , bacteria , hypoxanthine guanine phosphoribosyltransferase , biology , genetics , gene , organic chemistry , mutant , polymer
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 Å 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.