1WV4

X-ray Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in tetragonal crystal form

Summary for 1WV4

• Entry DOI: 10.2210/pdb1wv4/pdb
• Related: 1DNL 1G79 1JNW
• Descriptor: Pyridoxamine 5'-phosphate oxidase, PHOSPHATE ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: plp, fmn, pyridoxal, pyridoxine 5'-phosphate, oxidase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 52273.01

Authors

Safo, M.K.,Musayev, F.N.,Schirch, V. (deposition date: 2004-12-11, release date: 2004-12-28, Last modification date: 2023-10-25)

Primary citation

Safo, M.K.,Musayev, F.N.,Schirch, V.
Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme.
Acta Crystallogr.,Sect.D, 61:599-604, 2005

PubMed Abstract: Escherichia coli pyridoxine 5'-phosphate oxidase (ePNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP) by the FMN oxidation of pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP), forming FMNH(2) and H(2)O(2). The crystal structure of ePNPOx is reported in a tetragonal unit cell at 2.6 A resolution. The three-dimensional fold of this structure is very similar to those of the E. coli and human enzymes that crystallized in trigonal and monoclinic unit cells. However, unlike the previous structures, the tetragonal structure shows major disorder in one of the two subunit domains that has opened up both the active site and a putative tunnel. Comparison of these structures gives an insight into the mechanistic pathway of PNPOx: from the resting enzyme with no substrate bound, to the initial binding of the substrate at the active site, to the catalytic stage and to the release of the catalytic product from the active site.

PubMed: 15858270
DOI: 10.1107/S0907444905005512

Experimental method

X-RAY DIFFRACTION (2.6 Å)