1DNL

X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH FMN AT 1.8 ANGSTROM RESOLUTION

Summary for 1DNL

• Entry DOI: 10.2210/pdb1dnl/pdb
• Descriptor: PYRIDOXINE 5'-PHOSPHATE OXIDASE, PHOSPHATE ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: beta barrel, protein-fmn complex, oxidoreductase
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 23990.50

Authors

Safo, M.K.,Mathews, I.,Musayev, F.N.,di Salvo, M.L.,Thiel, D.J.,Abraham, D.J.,Schirch, V. (deposition date: 1999-12-16, release date: 2000-01-05, Last modification date: 2024-10-09)

Primary citation

Safo, M.K.,Mathews, I.,Musayev, F.N.,di Salvo, M.L.,Thiel, D.J.,Abraham, D.J.,Schirch, V.
X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution.
Structure Fold.Des., 8:751-762, 2000

PubMed Abstract: Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high degree of sequence homology among the 15 known members of the PNPOx family suggests that all members of this group have similar three-dimensional folds.

PubMed: 10903950
DOI: 10.1016/S0969-2126(00)00162-3

Experimental method

X-RAY DIFFRACTION (1.8 Å)