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Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.

Authors :
Liu, Chao-Pei
Xu, Rui
Gao, Zeng-Qiang
Xu, Jian-Hua
Hou, Hai-Feng
Li, Li-Qin
She, Zhun
Li, Lan-Fen
Su, Xiao-Dong
Liu, Peng
Dong, Yu-Hui
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). May2010, Vol. 66 Issue 5, p498-502. 5p.
Publication Year :
2010

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 Å 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
66
Issue :
5
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
111657263
Full Text :
https://doi.org/10.1107/S1744309110009243