1ow2

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1ow2, resolution 2.00Å

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STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP

Overview

Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is, a key enzyme in the biosynthesis of isoprenoids. The mechanism of the, isomerization reaction involves protonation of the unactivated, carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal, structure of the inactive C67A mutant of E. coli isopentenyl, diphosphate:dimethylallyl diphosphate isomerase complexed with the, mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in, agreement with an isomerization mechanism involving Glu 116, Tyr 104, and, Cys 67. In particular, the results are consistent with a mechanism where, Glu116 is involved in the protonation step and Cys67 in the elimination, step.

About this Structure

1OW2 is a Single protein structure of sequence from Escherichia coli with MN, MG and EIP as ligands. Active as Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor., Wouters J, Oudjama Y, Stalon V, Droogmans L, Poulter CD, Proteins. 2004 Feb 1;54(2):216-21. PMID:14696183

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