1oxm

File:1oxm.gif

spinqualitylabelsall models 1oxm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF CUTINASE

OverviewOverview

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.

About this StructureAbout this Structure

1OXM is a Single protein structure of sequence from Fusarium solani subsp. pisi with TC4 as ligand. Structure known Active Site: TC4. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cutinase covalently inhibited by a triglyceride analogue., Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C, Protein Sci. 1997 Feb;6(2):275-86. PMID:9041628

Page seeded by OCA on Mon Nov 5 16:58:52 2007