Crystal structure of cutinase covalently inhibited by a triglyceride analogue

Protein Science

Volumn 6, Issue 2, 1997, Pages 275-286

  Longhi, Sonia ^a   Mannesse, Maurice ^b,d   Verheij, Hubertus M ^b,d   De Haas, Gerard H ^b,d   Egmond, Maarten ^c   Knoops Mouthuy, Edith ^a   Cambillau, Christian ^a  

^a Centre National de la Recherche Scientifique   (France)

^b Transitonum III   (Netherlands)

^c UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

^d UTRECHT UNIVERSITY   (Netherlands)

Author keywords

covalently inhibited complex; cutinase; tetrahedral intermediate analogue; triglyceride analogue; X ray crystallography

Indexed keywords

1,2 DIBUTYLCARBAMOYLGLYCERO 3 O 4 NITROPHENYLBUTYLPHOSPHONATE; CUTINASE; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

ARTICLE; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME INHIBITION; FUSARIUM; INHIBITION KINETICS; PRIORITY JOURNAL;

EID: 0031055628     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060202     Document Type: Article

References (47)

1. Abergel C, Martinez C, Fontecilla-Camps J, Cambillau C, De Geus P, Lauwereys M. 1990. Crystallization and preliminary X-ray study of a recombinant cutinase from Fusarium solani pisi. J Mol Biol 215:215-216.
2. Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson GG, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U. 1990. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 346:767-770.
3. Brünger AT. 1993. X-PLOR version 3.1 Manual. New Haven, CT: Yale University.
4. Brzozowski AM, Derewenda U, Drewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjokling F, Huge-Jensen B, Patkar SA, Thim L. 1991. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351:491-494.
5. Cambillau C, van Tilbeurgh H. 1993. Structure of hydrolases: Lipases and cellulases. Curr Opin Struct Biol 3:885-895.
6. Cambillau C, Longhi S, Nicolas A, Martinez C. 1996. Acyl glycerol hydrolases: Inhibitors, interface and catalysis. Curr Opin Struct Biol 6:449-455.
7. Cygler M, Grochulski P, Kazlauskas RJ, Schrag JD, Bouthillier F, Rubin B, Serreqi AN, Gupta AK. 1994. A structural basis for the chiral preference of lipases. J Am Chem Soc 116:3180-3186.
8. Derewenda U, Brzozowski AM, Lawson D, Derewenda ZS. 1992. Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase. Biochemistry 31:1532-1541.
9. Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H. 1995. The 2.46 Å resolution structure of the pancreatic lipase-procolipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34:2751-2762.
10. Ghosh D, Wawrzak Z, Pletnev VZ, Li N, Kaiser R, Pangborn W, Jörnvall H, Erman M, Duax WL. 1995. Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase. Structure 3:279-288.
11. Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M. 1993. Insights into interfacial activation from an open structure of Candida rugosa lipase. J Biol Chem 268:12843-12847.
12. Grochulski P, Li Y, Schrag JD, Cygler M. 1994a. Two conformational states of Candida rugosa lipase. Protein Sci 3:82-91.
13. Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M. 1994b. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry 33:3494-3500.
14. Hermoso J, Pignol D, Kerfelec B, Crenon I, Chapus C, Fontecilla-Camps JC. 1996. Lipase activation by non-ionic detergents. The crystal structure of porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J Biol Chem 271:18007-18016.
15. Hodel A, Kim SH, Brünger A. 1992. Model bias in macromolecular crystal structures. Acta Crystallogr A 48:851-858.
16. Kabsch W. 1988a. Automatic indexing of rotation diffraction patterns. J Appl Crystallogr 21:67-71.
17. Kabsch W. 1988b. Evaluation of single crystal X-ray diffraction from a position-sensitive detector. J Appl Crystallogr 21:916-924.
18. Kolattukudy PE. 1984. Cutinase from fungi and pollen. In: Borgstrom B, Brockman H., eds. Lipases. Amsterdam: Elsevier. pp 471-504.
19. Kraut J. 1977. Serine proteases: Structure and mechanism of catalysis. Annu Rev Biochem 46:331-358.
20. Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schoburg D. 1996. Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 Å resolution. J Mol Biol 259:704-717.
21. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283-291.
22. Lauwereys M, De Geus P, De Meuter J, Stanssens P, Matthyssens G. 1991. Cloning, expression and characterization of cutinase, a fungal lipolytic enzyme. In: Alberghina L, Schmidt R, Verger R, eds. Lipases structure & Mechanical Genetic Engineering, Vol. 16. Wenheim, Germany: VCH. pp 243-225.
23. Lawson DM, Brzozowski AM, Dodson GG. 1992. Lifting the lid off upases. Curr Opin Struct Biol 9:473-475.
24. Mannesse MLM, Cox RC, Koops BC, Verheij HM, de Haas GH, Egmond M, van der Hijden HTWM, de Vlieg J. 1995a. Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry 34:6400-6407.
25. Mannesse MLM, Boots JWP, Dijkman R, Slotboom AJ, van der Hijden HTWM, Egmond M, Verheij HM, de Haas GH. 1995b. Phosphonate analogues of triacylglycerols are potent inhibitors of lipase. Biochim Biophys Acta 1259:56-64.
26. Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C. 1992. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to the solvent. Nature 356:615-618.
27. Martinez C, De Geus P, Stanssens P, Lauwereys M, Cambillau C. 1993. Engineering cysteine mutants to obtain crystallographic phases with a cutinase from Fusarium solani pisi. Protein Eng 6:157-165.
28. Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C. 1994. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33:83-89.
29. Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A 50:157-163.
30. Nicolas A, Egmond M, Verrips CT, Longhi S, Cambillau C, Martinez C. 1996. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry 35:398-410.
31. Noble MEM, Cleasby A, Johnson LN, Egmond MR, Frenken LGJ. 1993. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett 331:123-128.
32. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Shrag J, Sussman JL, Verschueren KHG, Goldman A. 1992. The α/β hydrolase fold. Protein Eng 5:197-211.
33. Read RJ. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
34. Rogalska E, Nury S, Douchet I, Verger R. 1995. Lipase stereoselectivity and regioselectivity toward three isomers of dicaprin: A kinetic study by the monomolecular film technique. Chirality 7:505-515.
35. Roussel A, Cambillau C. 1991. In: Silicon graphics geometry partners directory. Mountain View, CA: Silicon Graphics. p 86.
36. Sarda L, Desnuelle P. 1958. Action de la lipase pancréatique sur les esters en émulsion. Biochim Biophys Acta 50:513-521.
37. Schrag JD, Li Y, Wu S, Cygler M. 1991. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 357:761-764.
38. Schrag JD, Cygler M. 1993. 1.8 Å refined structure of the lipase from Geotrichum candidum. J Mol Biol 230:575-591.
39. Smith LC, Faustinella F, Lawrence C. 1992. Lipases: Three-dimensional structure and mechanism of action. Curr Opin Struct Biol 2:490-496.
40. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. 1991. Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science 253:872-879.
41. Uppenberg J, Hansen MT, Patkar S, Jones TA. 1994. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2:293-308.
42. Uppenberg J, Öhrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA. 1995. Crystallographic and molecular modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 34:16838-16851.
43. van Tilbeurgh H, Sarda L, Verger R, Cambillau C. 1992. Structure of the pancreatic lipase-procolipase complex. Nature 359:159-162.
44. van Tilbeurg H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C. 1993. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 362:814-820.
45. Verger R, De Haas GH. 1976. Interfacial enzyme kinetics of lipolysis. Annu Rev Biophys Bioeng 5:77-117.
46. Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS. 1995. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nat Struct Biol 2:218-223.
47. Winkler FK, D'Arcy A, Hunziker W. 1990. Structure of human pancreatic lipase. Nature 343:771-774.