1oxm

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 ... [(full description)]

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

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