1OW2

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

Summary for 1OW2

• Entry DOI: 10.2210/pdb1ow2/pdb
• Descriptor: ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE, MANGANESE (II) ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: complex, isomerase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: Q46822
• Total number of polymer chains: 2
• Total formula weight: 41911.35

Authors

Wouters, J. (deposition date: 2003-03-28, release date: 2004-01-20, Last modification date: 2024-11-13)

Primary citation

Wouters, J.,Oudjama, Y.,Stalon, V.,Droogmans, L.,Poulter, C.D.
Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor
Proteins, 54:216-221, 2004

PubMed 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 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.

PubMed: 14696183
DOI: 10.1002/prot.10573

Experimental method

X-RAY DIFFRACTION (2 Å)