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1g77
From Proteopedia
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X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION
Overview
Escherichia coli pyridoxine 5'-phosphate oxidase catalyzes the terminal, step in the biosynthesis of pyridoxal 5'-phosphate by the FMN oxidation of, pyridoxine 5'-phosphate forming FMNH(2) and H(2)O(2). Recent studies have, shown that in addition to the active site, pyridoxine 5'-phosphate oxidase, contains a non-catalytic site that binds pyridoxal 5'-phosphate tightly., The crystal structure of pyridoxine 5'-phosphate oxidase from E. coli with, one or two molecules of pyridoxal 5'-phosphate bound to each monomer has, been determined to 2.0 A resolution. One of the pyridoxal 5'-phosphate, molecules is clearly bound at the active site with the aldehyde at C4' of, pyridoxal 5'-phosphate near N5 of the bound FMN. A protein conformational, change has occurred that partially closes the active site. The orientation, of the bound pyridoxal 5'-phosphate suggests that the enzyme catalyzes a, hydride ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN., When the crystals are soaked with excess pyridoxal 5'-phosphate an, additional molecule of this cofactor is also bound about 11 A from the, active site. A possible tunnel exists between the two sites so that, pyridoxal 5'-phosphate formed at the active site may transfer to the, non-catalytic site without passing though the solvent.
About this Structure
1G77 is a Single protein structure of sequence from Escherichia coli with PO4, FMN and PLP as ligands. Active as Pyridoxal 5'-phosphate synthase, with EC number 1.4.3.5 Full crystallographic information is available from OCA.
Reference
X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution., Safo MK, Musayev FN, di Salvo ML, Schirch V, J Mol Biol. 2001 Jul 20;310(4):817-26. PMID:11453690
Page seeded by OCA on Tue Nov 20 15:46:33 2007
