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Updated: Jun 13, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans
Chao Pei Liu1, Rui Xu, Zeng Qiang Gao
1Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
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.
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