1rm0
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(New page: 200px<br /><applet load="1rm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rm0, resolution 2.05Å" /> '''Crystal Structure of...)
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Revision as of 23:34, 20 November 2007
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Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate
Overview
1l-myo-inositol 1-phosphate (MIP) synthase catalyzes the conversion of, d-glucose 6-phosphate to 1l-myo-inositol 1-phosphate, the first and, rate-limiting step in the biosynthesis of all inositol-containing, compounds. It involves an oxidation, enolization, intramolecular aldol, cyclization, and reduction. Here we present the structure of MIP synthase, in complex with NAD(+) and a high-affinity inhibitor, 2-deoxy-d-glucitol, 6-(E)-vinylhomophosphonate. This structure reveals interactions between, the enzyme active site residues and the inhibitor that are significantly, different from that proposed for 2-deoxy-d-glucitol 6-phosphate in the, previously published structure of MIP synthase-NAD(+)-2-deoxy-d-glucitol, 6-phosphate. There are several other conformational changes in NAD(+) and, the enzyme active site as well. Based on the new structural data, we, propose a new and completely different mechanism for MIP synthase.
About this Structure
1RM0 is a Single protein structure of sequence from Saccharomyces cerevisiae with MN, D6P 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 structure of the 1L-myo-inositol-1-phosphate synthase-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism., Jin X, Foley KM, Geiger JH, J Biol Chem. 2004 Apr 2;279(14):13889-95. Epub 2003 Dec 18. PMID:14684747
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