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

Proteins: Structure, Function and Genetics

Volumn 54, Issue 2, 2004, Pages 216-221

  Wouters, Johan ^a,b   Oudjama, Y ^a   Stalon, V ^a,b   Droogmans, L ^b   Poulter, C D ^c  

^a Inst de Rech Microbiol JM Wiame   (Belgium)

^b Laboratoire de Microbiologie   (Belgium)

^c UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3,4 EPOXY 3 METHYL 1 BUTYL DIPHOSPHATE; CYSTEINE; GLUTAMINE; ISOPENTENYL DIPHOSPHATE DELTA ISOMERASE; ISOPRENOID; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BINDING; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; ISOMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ANALYSIS;

BINDING SITES; CARBON-CARBON DOUBLE BOND ISOMERASES; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; EPOXY COMPOUNDS; ESCHERICHIA COLI; ISOMERISM; ORGANOPHOSPHORUS COMPOUNDS; POINT MUTATION; PROTONS;

EID: 0346458808     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10573     Document Type: Article

References (13)

1. Durbecq V, Sainz G, Oudjama Y, Clantin B, Bompard-Gilles C, Tricot C, Caillet J, Stalon V, Droogmans L, Villeret V. Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isornerase. EMBO J 2001;20:1530-1537.
2. Wouters J, Oudjama Y, Barkley S, Tricot C, Stalon V, Droogmans L, Poulter CD. Catalytic mechanism of E. coli isopentenyl diphosphate isomerase involves Cys67, Glu116 and Tyr104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors. J Biol Chem 2003. Forthcoming.
3. Wouters J, Oudjama Y, Ghosh S, Stalon V, Droogmans L, Oldfield E. Structure and Mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase. J Am Chem Soc 2003;125:3198-3199.
4. Sheldrick GM, Schneider TR. Shelxl: high resolution refinement. Carter C, Sweet R, editors. In Methods in Enzymology vol. 277, Academic Press; 1997 p. 319-343.
5. Roussel A, Cambillau C. Turbo-Frodo. Marsseille, France: Biographics, AFMB, 1992.
6. Cambridge Crystallographic Data Centre, Relibase: A program for searching protein-ligand databases; Cambridge, UK: 2000.
7. Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK. Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Proc Natl Acad Sci USA. 2001;98:12896-12901.
8. Muehlbacher M, Poulter CD. Isopentenyl-diphosphate isomerase: inactivation of the enzyme with active-site-directed irreversible inhibitors and transition-state analogues. Biochemistry 1988;27:7315-7328.
9. Street IP, Coffman HR, Baker JA, Poulter CD. Identification of Cys139 and Glu207 as catalytically important groups in the active site of isopentenyl diphosphate:dimethylallyl diphosphate isomerase. Biochemistry 1994;33:4212-4217.
10. Leyes AE, Baker JA, Poulter CD. Biosynthesis of isoprenoids in Escherichia coli: stereochemistry of the reaction catalyzed by farnesyl diphosphate synthase. Org Lett 1999;1:1071-1073.
11. Muehlbacher M, Poulter CD. Isopentenyl-diphosphate isomerase: Irreversible inhibition of the enzyme by active-site directed covalent attachment. J Am Chem Soc 1985;107:8307-8308.
12. Street IP, Poulter CD. Isopentenyldiphosphate:dimethylallyl-diphosphate isomerase: construction of a high-level heterologous expression system for the gene from Saccharomyces cerevisiae and identification of an active-site nucleophile. Biochemistry 1990;29:7531-7538.
13. Harding M. Geometry of metal-ligand interactions in proteins Acta Crystallogr D 2001;57:401-411.