1jki
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(New page: 200px<br /><applet load="1jki" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jki, resolution 2.2Å" /> '''myo-Inositol-1-phosph...)
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Revision as of 16:13, 20 November 2007
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myo-Inositol-1-phosphate Synthase Complexed with an Inhibitor, 2-deoxy-glucitol-6-phosphate
Overview
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.
About this Structure
1JKI is a Single protein structure of sequence from Saccharomyces cerevisiae with NH4, DG6 and NAI as ligands. Active as Inositol-3-phosphate synthase, with EC number 5.5.1.4 Full crystallographic information is available from OCA.
Reference
The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate synthase., Stein AJ, Geiger JH, J Biol Chem. 2002 Mar 15;277(11):9484-91. Epub 2002 Jan 4. PMID:11779862
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