Cutinase from Fusarium solani is a lipolytic enzyme that hydrolyses
triglycerides efficiently All the inhibited forms of lipolytic enzymes described
so far are based on the use of small organophosphate
and organophosphonate inhibitors which bear little resemblance to a natural
triglyceride substrate In this article we describe the crystal structure
of cutinase covalently inhibited by R)-1,2-dibutyl carbamoylglycero-3-O-p-nitrophenylbutyl-phos phonate a triglyceride
analogue mimicking the first tetrahedral intermediate along the reaction pathway
The structure which has been solved at 2.3 A reveals
that in both the protein molecules of the asymmetric unit
the inhibitor is almost completely embedded in the active site
crevice The overall shape of the inhibitor is that of
a fork the two dibutyl carbamoyl chains point towards the
surface of the protein whereas the butyl chain bound to
the phosphorous atom is roughly perpendicular to the sn-1 and
sn-2 chains The sn-3 chain is accommodated in a rather
small pocket at the bottom of the active site crevice
thus providing a structural explanation for the preference of cutinase
for short acyl chain substrates
        
Representative scheme of Cutinase structure and an image from PDBsum server
Databases
PDB-Sum
1FFE Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
1FFEFold classification based on Structure-Structure alignment of Proteins - FSSP server