3DEZ

Crystal structure of Orotate phosphoribosyltransferase from Streptococcus mutans

Summary for 3DEZ

Entry DOI	10.2210/pdb3dez/pdb
Descriptor	Orotate phosphoribosyltransferase, SULFATE ION (3 entities in total)
Functional Keywords	orotate phosphoribosyltransferase, glycosyltransferase, magnesium, pyrimidine biosynthesis, transferase
Biological source	Streptococcus mutans
Total number of polymer chains	2
Total formula weight	53106.43
Authors	Liu, C.P.,Gao, Z.Q.,Hou, H.F.,Li, L.F.,Su, X.D.,Dong, Y.H. (deposition date: 2008-06-11, release date: 2009-06-16, Last modification date: 2023-11-01)
Primary citation	Liu, C.P.,Xu, R.,Gao, Z.Q.,Xu, J.H.,Hou, H.F.,Li, L.Q.,She, Z.,Li, L.F.,Su, X.D.,Liu, P.,Dong, Y.H. Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans Acta Crystallogr.,Sect.F, 66:498-502, 2010 Cited by PubMed 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. PubMed: 20445243 DOI: 10.1107/S1744309110009243 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation