1DEA

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

Summary for 1DEA

• Entry DOI: 10.2210/pdb1dea/pdb
• Descriptor: GLUCOSAMINE 6-PHOSPHATE DEAMINASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: intramolecular oxidoreductase deaminase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 60004.31

Authors

Oliva, G.,Fontes, M.R.M.,Garratt, R.C.,Altamirano, M.M.,Calcagno, M.L.,Horjales, E. (deposition date: 1995-09-13, release date: 1996-01-29, Last modification date: 2024-02-07)

Primary citation

Oliva, G.,Fontes, M.R.,Garratt, R.C.,Altamirano, M.M.,Calcagno, M.L.,Horjales, E.
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
Structure, 3:1323-1332, 1995

PubMed Abstract: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function.

PubMed: 8747459
DOI: 10.1016/S0969-2126(01)00270-2

Experimental method

X-RAY DIFFRACTION (2.1 Å)