1HO4

CRYSTAL STRUCTURE OF PYRIDOXINE 5'-PHOSPHATE SYNTHASE IN COMPLEX WITH PYRIDOXINE 5'-PHOSPHATE AND INORGANIC PHOSPHATE

Summary for 1HO4

• Entry DOI: 10.2210/pdb1ho4/pdb
• Related: 1HO1
• Descriptor: PYRIDOXINE 5'-PHOSPHATE SYNTHASE, PHOSPHATE ION, PYRIDOXINE-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: tim barrel, open-closed transition, enzyme-product complex, water channel, biosynthetic protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A794
• Total number of polymer chains: 4
• Total formula weight: 106442.12

Authors

Garrido-Franco, M.,Laber, B.,Huber, R.,Clausen, T. (deposition date: 2000-12-08, release date: 2001-03-28, Last modification date: 2024-04-03)

Primary citation

Franco, M.G.,Laber, B.,Huber, R.,Clausen, T.
Structural basis for the function of pyridoxine 5'-phosphate synthase.
Structure, 9:245-253, 2001

PubMed Abstract: Pyridoxal 5'-phosphate is the active form of vitamin B(6) that acts as an essential, ubiquitous coenzyme in amino acid metabolism. In Escherichia coli, the pathway of the de novo biosynthesis of vitamin B(6) results in the formation of pyridoxine 5'-phosphate (PNP), which can be regarded as the first synthesized B(6) vitamer. PNP synthase (commonly referred to as PdxJ) is a homooctameric enzyme that catalyzes the final step in this pathway, a complex intramolecular condensation reaction between 1-deoxy-D-xylulose-5'-phosphate and 1-amino-acetone-3-phosphate.

PubMed: 11286891
DOI: 10.1016/S0969-2126(01)00584-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)