A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens.

@article{Meier2007ACL,
  title={A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens.},
  author={Reto Meier and Thomas Drepper and Vera Svensson and Karl-Erich Jaeger and Ulrich Baumann},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 43},
  pages={
          31477-83
        }
}
Lipase LipA from Serratia marcescens is a 613-amino acid enzyme belonging to family I.3 of lipolytic enzymes that has an important biotechnological application in the production of a chiral precursor for the coronary vasodilator diltiazem. Like other family I.3 lipases, LipA is secreted by Gram-negative bacteria via a type I secretion system and possesses 13 copies of a calcium binding tandem repeat motif, GGXGXDXUX (U, hydrophobic amino acids), in the C-terminal part of the polypeptide chain… CONTINUE READING

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