1JKF

Holo 1L-myo-inositol-1-phosphate Synthase

Summary for 1JKF

• Entry DOI: 10.2210/pdb1jkf/pdb
• Related: 1JKI
• Descriptor: myo-inositol-1-phosphate synthase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: rossmann fold, isomerase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P11986
• Total number of polymer chains: 2
• Total formula weight: 120742.38

Authors

Stein, A.J.,Geiger, J.H. (deposition date: 2001-07-12, release date: 2002-04-10, Last modification date: 2024-12-25)

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

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: 11779862
DOI: 10.1074/jbc.M109371200

Experimental method

X-RAY DIFFRACTION (2.4 Å)