Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.
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.
Liu
Chao Pei
CP
Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
Xu
Rui
R
Gao
Zeng Qiang
ZQ
Xu
Jian Hua
JH
Hou
Hai Feng
HF
Li
Li Qin
LQ
She
Zhun
Z
Li
Lan Fen
LF
Su
Xiao Dong
XD
Liu
Peng
P
Dong
Yu Hui
YH
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*
D009962:Orotate Phosphoribosyltransferase
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