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Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans.
- 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