1jxa
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(New page: 200px<br /><applet load="1jxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxa, resolution 3.1Å" /> '''GLUCOSAMINE 6-PHOSPHA...)
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Revision as of 16:32, 20 November 2007
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GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE
Overview
Glucosamine-6-phosphate synthase catalyses the first and rate-limiting, step in hexosamine metabolism, converting fructose 6-phosphate into, glucosamine 6-phosphate in the presence of glutamine. The crystal, structure of the Escherichia coli enzyme reveals the domain organisation, of the homodimeric molecule. The 18 A hydrophobic channel sequestered from, the solvent connects the glutaminase and isomerase active sites, and, provides a means of ammonia transfer from glutamine to sugar phosphate., The C-terminal decapeptide sandwiched between the two domains plays a, central role in the transfer. Based on the structure, a mechanism of, enzyme action and self-regulation is proposed. It involves large domain, movements triggered by substrate binding that lead to the formation of the, channel.
About this Structure
1JXA is a Single protein structure of sequence from Escherichia coli with G6Q as ligand. Active as Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16 Full crystallographic information is available from OCA.
Reference
Channeling of ammonia in glucosamine-6-phosphate synthase., Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA, J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065
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