Summary for 4AMV
| Entry DOI | 10.2210/pdb4amv/pdb |
| Related | 4AMK |
| Descriptor | GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMER IZING], FRUCTOSE -6-PHOSPHATE (3 entities in total) |
| Functional Keywords | transferase, ammonia channeling, glucosamine 6- phosphate synthase, n terminal nucleophile, glutamine amidotransferase |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm: P17169 |
| Total number of polymer chains | 3 |
| Total formula weight | 201627.99 |
| Authors | Mouilleron, S.,Golinelli-Pimpaneau, B. (deposition date: 2012-03-14, release date: 2013-04-24, Last modification date: 2023-12-20) |
| Primary citation | Mouilleron, S.,Badet-Denisot, M.A.,Golinelli-Pimpaneau, B. Glutamine Binding Opens the Ammonia Channel and Activates Glucosamine-6P Synthase J.Biol.Chem., 281:4404-, 2006 Cited by 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: 16339762DOI: 10.1074/JBC.M511689200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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