Download MendeleyMultistate Binding in Pyridoxine 5'-Phosphate Synthase: 1.96 A Crystal Structure in Complex with 1-deoxy-D-xylulose phosphate
Yeh, J.I., Du, S., Pohl, E., Cane, D.E.(2002) Biochemistry 41: 11649-11657
- PubMed: 12269807
- DOI: https://doi.org/10.1021/bi026292t
- Primary Citation of Related Structures:
1M5W - PubMed Abstract:
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 binding states are observed. The observation of these three states supports a mechanism in which precise conformational changes of a peptide loop and groups of active site residues modulate binding and specificity. The differences in protein conformation when one or two substrates are bound can be correlated with a condensation mechanism that leads productively to the formation of pyridoxine 5'-phosphate (PNP). "Snapshots" of the progression from the apo form to a singly occupied "transitional binding" state and, subsequently, to a fully occupied, reactive state are revealed and indicate how the enzyme structure can be related to a plausible catalytic mechanism and, moreover, to favorable energetics of reaction.
Organizational Affiliation:
Molecular Biology, Cell Biology, and Biochemistry Department, Brown University, Box G-J2, Providence, RI 02912-9108, USA. Joanne_Yeh@brown.edu
