title: Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.
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.
authors.affiliation: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
authors.forename: Chao Pei
authors.initials: CP
authors.lastname: Liu
authors.forename: Rui
authors.initials: R
authors.lastname: Xu
authors.forename: Zeng Qiang
authors.initials: ZQ
authors.lastname: Gao
authors.forename: Jian Hua
authors.initials: JH
authors.lastname: Xu
authors.forename: Hai Feng
authors.initials: HF
authors.lastname: Hou
authors.forename: Li Qin
authors.initials: LQ
authors.lastname: Li
authors.forename: Zhun
authors.initials: Z
authors.lastname: She
authors.forename: Lan Fen
authors.initials: LF
authors.lastname: Li
authors.forename: Xiao Dong
authors.initials: XD
authors.lastname: Su
authors.forename: Peng
authors.initials: P
authors.lastname: Liu
authors.forename: Yu Hui
authors.initials: YH
authors.lastname: Dong
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009962:Orotate Phosphoribosyltransferase / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: D009962:Orotate Phosphoribosyltransferase
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