1n8t
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(New page: 200px<br /><applet load="1n8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n8t, resolution 2.50Å" /> '''The crystal structur...)
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Revision as of 19:56, 20 November 2007
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The crystal structure of phosphoglucose isomerase from rabbit muscle
Overview
Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that, catalyses the interconversion of glucose 6-phosphate and fructose, 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI, is also a multifunctional protein that manifests the properties of a, cytokine in a wide array of cellular processes, including the production, of immunoglobulin by B cells and tumour-cell differentiation. The crystal, structure of PGI in the native form from rabbit muscle has been solved at, a resolution of 2.5 A by a combination of multiple isomorphous replacement, and multi-crystal averaging techniques. Comparison with published, structures of rabbit PGI in complex with three inhibitors and with the, substrate fructose 6-phosphate reveals a number of conformational changes, that may be associated with catalytic function. These occur in the small, domain around the sugar phosphate-binding site, in a small helix carrying, His388 and in a helix near the C-terminal end. One of these may be the, structural rearrangement that has been postulated to be the rate-limiting, step for catalysis.
About this Structure
1N8T is a Single protein structure of sequence from Oryctolagus cuniculus. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
Reference
Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function., Davies C, Muirhead H, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):453-65. Epub 2003, Feb 21. PMID:12595702
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