| Literature DB >> 20445243 |
Chao Pei Liu1, Rui Xu, Zeng Qiang Gao, Jian Hua Xu, Hai Feng Hou, Li Qin Li, Zhun She, Lan Fen Li, Xiao Dong Su, Peng Liu, Yu Hui Dong.
Abstract
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.Entities:
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Year: 2010 PMID: 20445243 PMCID: PMC2864676 DOI: 10.1107/S1744309110009243
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091