1JXA
GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE
Summary for 1JXA
| Entry DOI | 10.2210/pdb1jxa/pdb |
| Related | 1gdo 1moq |
| Descriptor | glucosamine 6-phosphate synthase, GLUCOSE-6-PHOSPHATE (3 entities in total) |
| Functional Keywords | beta-sandwich, nucleotide-binding fold, gene duplication, ammonia channel, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 200974.27 |
| Authors | Teplyakov, A.,Obmolova, G.,Badet, B.,Badet-Denisot, M.A. (deposition date: 2001-09-06, release date: 2001-11-21, Last modification date: 2024-12-25) |
| Primary citation | Teplyakov, A.,Obmolova, G.,Badet, B.,Badet-Denisot, M.A. Channeling of ammonia in glucosamine-6-phosphate synthase. J.Mol.Biol., 313:1093-1102, 2001 Cited by PubMed Abstract: 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. PubMed: 11700065DOI: 10.1006/jmbi.2001.5094 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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