1MOQ

ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE

Summary for 1MOQ

• Entry DOI: 10.2210/pdb1moq/pdb
• Descriptor: GLUCOSAMINE 6-PHOSPHATE SYNTHASE, 2-amino-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, SULFATE ION, ... (7 entities in total)
• Functional Keywords: glutamine amidotransferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P17169
• Total number of polymer chains: 1
• Total formula weight: 41432.87

Authors

Teplyakov, A. (deposition date: 1997-04-11, release date: 1998-10-07, Last modification date: 2024-05-22)

Primary citation

Teplyakov, A.,Obmolova, G.,Badet-Denisot, M.A.,Badet, B.,Polikarpov, I.
Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.
Structure, 6:1047-1055, 1998

PubMed Abstract: Glucosamine 6-phosphate synthase (GlmS) catalyses the first step in hexosamine metabolism, converting fructose-6P (6 phosphate) into glucosamine-6P using glutamine as a nitrogen source. GlmS is a bienzyme complex consisting of two domains that catalyse glutamine hydrolysis and sugar-phosphate isomerisation, respectively. Knowledge of the three-dimensional structure of GlmS is essential for understanding the general principles of catalysis by ketol isomerases and the mechanism of nitrogen transfer in glutamine amidotransferases.

PubMed: 9739095
DOI: 10.1016/S0969-2126(98)00105-1

Experimental method

X-RAY DIFFRACTION (1.57 Å)