1JKI
myo-Inositol-1-phosphate Synthase Complexed with an Inhibitor, 2-deoxy-glucitol-6-phosphate
Summary for 1JKI
| Entry DOI | 10.2210/pdb1jki/pdb |
| Related | 1JKF |
| Descriptor | myo-inositol-1-phosphate synthase, AMMONIUM ION, 2-DEOXY-GLUCITOL-6-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | rossmann fold, inhibitor-bound structure, isomerase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm: P11986 |
| Total number of polymer chains | 2 |
| Total formula weight | 121274.79 |
| Authors | Stein, A.J.,Geiger, J.H. (deposition date: 2001-07-12, release date: 2002-04-10, Last modification date: 2023-08-16) |
| Primary citation | Stein, A.J.,Geiger, J.H. The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate synthase J.Biol.Chem., 277:9484-9491, 2002 Cited by PubMed Abstract: 1-l-myo-Inositol-1-phosphate synthase catalyzes the conversion of d-glucose 6-phosphate to 1-l-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. It involves an oxidation, intramolecular aldol cyclization, and reduction. We have determined the first crystal structure of MIP synthase. We present structures of both the NAD-bound enzyme and the enzyme bound to an inhibitor, 2-deoxy-glucitol-6-phosphate. While 58 amino acids are disordered in the unbound form of the enzyme in the vicinity of the active site, the inhibitor nucleates the folding of this domain in a striking example of induced fit, serving to completely encapsulate it within the enzyme. Three helices and a long beta-strand are formed in this process. We postulate a mechanism for the conversion based on the structure of the inhibitor-bound complex. PubMed: 11779862DOI: 10.1074/jbc.M109371200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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