1COZ

CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS

Summary for 1COZ

• Entry DOI: 10.2210/pdb1coz/pdb
• Descriptor: PROTEIN (GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE), CYTIDINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: transferase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P27623
• Total number of polymer chains: 2
• Total formula weight: 31557.39

Authors

Weber, C.H.,Park, Y.S.,Sanker, S.,Kent, C.,Ludwig, M.L. (deposition date: 1999-05-29, release date: 1999-10-06, Last modification date: 2023-12-27)

Primary citation

Weber, C.H.,Park, Y.S.,Sanker, S.,Kent, C.,Ludwig, M.L.
A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis.
Structure Fold.Des., 7:1113-1124, 1999

PubMed Abstract: The formation of critical intermediates in the biosynthesis of lipids and complex carbohydrates is carried out by cytidylyltransferases, which utilize CTP to form activated CDP-alcohols or CMP-acid sugars plus inorganic pyrophosphate. Several cytidylyltransferases are related and constitute a conserved family of enzymes. The eukaryotic members of the family are complex enzymes with multiple regulatory regions or repeated catalytic domains, whereas the bacterial enzyme, CTP:glycerol-3-phosphate cytidylyltransferase (GCT), contains only the catalytic domain. Thus, GCT provides an excellent model for the study of catalysis by the eukaryotic cytidylyltransferases.

PubMed: 10508782
DOI: 10.1016/S0969-2126(99)80178-6

Experimental method

X-RAY DIFFRACTION (2 Å)