Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.

@article{Price2004CofactorinducedCR,
  title={Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.},
  author={Allen C Price and Yong-mei Zhang and Charles O Rock and Stephen W. White},
  journal={Structure},
  year={2004},
  volume={12 3},
  pages={417-28}
}
beta-Ketoacyl-acyl carrier protein reductase (FabG) is a key component in the type II fatty acid synthase system. The structures of Escherichia coli FabG and the FabG[Y151F] mutant in binary complexes with NADP(H) reveal that mechanistically important conformational changes accompany cofactor binding. The active site Ser-Tyr-Lys triad is repositioned into a… CONTINUE READING