6YQQ
ForT-PRPP complex
Summary for 6YQQ
Entry DOI | 10.2210/pdb6yqq/pdb |
Descriptor | ForT-PRPP complex, SODIUM ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | c-glycosidic bond, biosynthetic protein |
Biological source | Streptomyces kaniharaensis |
Total number of polymer chains | 1 |
Total formula weight | 37075.84 |
Authors | Naismith, J.H.,Gao, S. (deposition date: 2020-04-18, release date: 2020-05-20, Last modification date: 2024-05-01) |
Primary citation | Gao, S.,Radadiya, A.,Li, W.,Liu, H.,Zhu, W.,de Crecy-Lagard, V.,Richards, N.G.J.,Naismith, J.H. Uncovering the chemistry of C-C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex. Chem.Commun.(Camb.), 56:7617-7620, 2020 Cited by PubMed Abstract: The enzyme ForT catalyzes C-C bond formation between 5'-phosphoribosyl-1'-pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3,5-dicarboxylate to make a key intermediate in the biosynthesis of formycin A 5'-phosphate by Streptomyces kaniharaensis. We report the 2.5 Å resolution structure of the ForT/PRPP complex and locate active site residues critical for PRPP recognition and catalysis. PubMed: 32515440DOI: 10.1039/d0cc02834g PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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