作者: Joanne I. Yeh , Shoucheng Du , Ehmke Pohl , David E. Cane
DOI: 10.1021/BI026292T
关键词:
摘要: We report the 1.96 A crystal structure of pyridoxine 5'-phosphate synthase (PdxJ) in complex with 1-deoxy-D-xylulose phosphate (dXP). The octameric enzyme possesses eight distinct binding sites, and three different states are observed. observation these supports a mechanism which precise conformational changes peptide loop groups active site residues modulate specificity. differences protein conformation when one or two substrates bound can be correlated condensation that leads productively to formation (PNP). "Snapshots" progression from apo form singly occupied "transitional binding" state and, subsequently, fully occupied, reactive revealed indicate how related plausible catalytic moreover, favorable energetics reaction.