6K96
Crystal structure of Ari2
Summary for 6K96
| Entry DOI | 10.2210/pdb6k96/pdb |
| Descriptor | Five-membered-cyclitol-phosphate synthase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | nad binding, rossmann fold, oxidoreductase |
| Biological source | Streptomyces citricolor |
| Total number of polymer chains | 2 |
| Total formula weight | 82065.92 |
| Authors | Miyanaga, A.,Tsunoda, T.,Kudo, F.,Eguchi, T. (deposition date: 2019-06-14, release date: 2019-12-25, Last modification date: 2023-11-22) |
| Primary citation | Kudo, F.,Tsunoda, T.,Yamaguchi, K.,Miyanaga, A.,Eguchi, T. Stereochemistry in the Reaction of themyo-Inositol Phosphate Synthase Ortholog Ari2 during Aristeromycin Biosynthesis. Biochemistry, 58:5112-5116, 2019 Cited by PubMed Abstract: The -inositol-1-phosphate synthase (MIPS) ortholog Ari2, which is encoded in the aristeromycin biosynthetic gene cluster, catalyzes the formation of five-membered cyclitol phosphate using d-fructose 6-phosphate (F6P) as a substrate. To understand the stereochemistry during the Ari2 reaction , we carried out feeding experiments with (6)-d-[6-H]- and (6)-d-[6-H]glucose in the aristeromycin-producing strain . We observed retention of the H atom of (6)-d-[6-H]glucose and no incorporation of the H atom from (6)-d-[6-H]glucose in aristeromycin. This indicates that Ari2 abstracts the proton at C6 of F6P after oxidation of C5-OH by nicotinamide adenine dinucleotide (NAD) to generate the enolate intermediate, which then attacks the C2 ketone to form the C-C bond via aldol-type condensation. The reaction of Ari2 with (6)-d-[6-H]- and (6)-d-[6-H]F6P exhibited identical stereochemistry compared with that observed during the feeding experiments. Furthermore, analysis of the crystal structure of Ari2, including NAD as a ligand, revealed the active site of Ari2 to be similar to that of MIPS of , supporting the similarity of the reaction mechanisms of Ari2 and MIPS. PubMed: 31825604DOI: 10.1021/acs.biochem.9b00981 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
