Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution.

@article{Lawrence1995CrystalSO,
  title={Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution.},
  author={Catherine M. Lawrence and Victor W. Rodwell and Cynthia V Stauffacher},
  journal={Science},
  year={1995},
  volume={268 5218},
  pages={1758-62}
}
The rate-limiting step in cholesterol biosynthesis in mammals is catalyzed by 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, a four-electron oxidoreductase that converts HMG-CoA to mevalonate. The crystal structure of HMG-CoA reductase from Pseudomonas mevalonii was determined at 3.0 angstrom resolution by multiple isomorphous replacement. The structure reveals a tightly bound dimer that brings together at the subunit interface the conserved residues implicated in substrate binding… CONTINUE READING