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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.

SUBMITTER: Liu CP 

PROVIDER: S-EPMC2864676 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.

Liu Chao Pei CP   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  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100429 Pt 5


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. ...[more]

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