1NFS

STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP

Summary for 1NFS

• Entry DOI: 10.2210/pdb1nfs/pdb
• Related: 1NFZ
• 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: 41945.46

Authors

Wouters, J. (deposition date: 2002-12-16, release date: 2003-06-24, Last modification date: 2023-08-16)

Primary citation

Wouters, J.,Oudjama, Y.,Barkley, S.J.,Tricot, C.,Stalon, V.,Droogmans, L.,Poulter, C.D.
Catalytic Mechanism of Escherichia coli Isopentenyl Diphosphate Isomerase Involves Cys-67, Glu-116, and Tyr-104 as Suggested by Crystal Structures of Complexes with Transition State Analogues and Irreversible Inhibitors
J.Biol.Chem., 278:11903-11908, 2003

PubMed Abstract: Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Analysis of the crystal structures (2 A) of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate) indicates that Glu-116, Tyr-104, and Cys-67 are involved in the antarafacial addition/elimination of protons during isomerization. This work provides a new perspective about the mechanism of the reaction.

PubMed: 12540835
DOI: 10.1074/jbc.M212823200

Experimental method

X-RAY DIFFRACTION (1.96 Å)