2bpl

From Proteopedia

E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P

Overview

Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from, fructose-6P and glutamine and uses a channel to transfer ammonia from its, glutaminase to its synthase active site. X-ray structures of, glucosamine-6P synthase have been determined at 2.05 Angstroms resolution, in the presence of fructose-6P and at 2.35 Angstroms resolution in the, presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine, affinity analog that covalently modifies the N-terminal catalytic, cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate, formed during hydrolysis of glutamine. The fixation of the glutamine, analog activates the enzyme through several major structural changes: 1), the closure of a loop to shield the glutaminase site accompanied by, significant domain hinging, 2) the activation of catalytic residues, involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and, Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees, rotation of the Trp-74 indole group that opens the ammonia channel.

About this Structure

2BPL is a Single protein structure of sequence from Escherichia coli with F6R as ligand. Active as Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:16339762

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