Molecule of the Month
October 2007
An Enzyme on the b-Roll:
The Crystal Structure of Extracellular Lipase LipA from Serratia marcescens

The extracellular lipase LipA is a 65 kDa protein of 613 amino acid residues from gram-negative enteric bacterium Serratia marcescens belonging to lipase family I.3. LipA is a biotechnologically very important enzyme that catalyses with high enantioselectivity the asymmetric hydrolysis of a precursor of diltiazem, a major pharmaceutical for the treatment of heart diseases produced worldwide in an excess of 100 t a-1.
The first structure of a lipase family I.3 member reveals a modified α/β hydrolase fold including a calcium gated lid in an open conformation. The structure of the C-terminal part of the molecule discloses a novel unique feature which has been termed “β-roll sandwich” consisting of tandem repeats split into two groups and separated by a 70 residue spacer.

This work was carried out in the group of Prof. Ulrich Baumann.


  • R. Meier, T. Drepper, V. Svensson, K.-E. Jaeger, U. Baumann;
    "A Calcium-gated Lid and a Large b-Roll Sandwich Are Revealed by the Crystal Structure of Extracellular Lipase from Serratia marcescens"
    J. Biol. Chem., 282, 31477–31483, (2007); doi:10.1074/jbc.M704942200.