Crystal Structure of the C67A Mutant of Isopentenyl Diphosphate Isomerase Complexed with a Mechanism-Based Irreversible Inhibitor

Johan Wouters, Y. Oudjama, V. Stalon, L. Droogmans, C. D. Poulter

Research output: Contribution to journalArticle

Abstract

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 Å 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.

Original languageEnglish
Pages (from-to)216-221
Number of pages6
JournalProteins: Structure, Function and Genetics
Volume54
Issue number2
DOIs
Publication statusPublished - 1 Feb 2004

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