2J6H

E. coli glucosamine-6-P synthase in complex with glucose-6P and 5-oxo- L-norleucine

Replaces:  2BPJ

Summary for 2J6H

• Entry DOI: 10.2210/pdb2j6h/pdb
• Related: 1JXA 1MOQ 1MOR 1MOS 1XFF 1XFG 2BPL
• Descriptor: GLUCOSAMINE-FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, 5-OXO-L-NORLEUCINE, GLUCOSE-6-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase, ammonia channeling
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P17169
• Total number of polymer chains: 2
• Total formula weight: 134502.62

Authors

Mouilleron, S.,Golinelli-Pimpaneau, B. (deposition date: 2006-09-28, release date: 2006-10-02, Last modification date: 2023-12-13)

Primary citation

Mouilleron, S.,Badet-Denisot, M.A.,Golinelli-Pimpaneau, B.
Glutamine Binding Opens the Ammonia Channel and Activates Glucosamine-6-Phosphate Synthase.
J.Biol.Chem., 281:4404-, 2006

PubMed Abstract: 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.

PubMed: 16339762
DOI: 10.1074/JBC.M511689200

Experimental method

X-RAY DIFFRACTION (2.35 Å)