Packing forces in nine crystal forms of cutinase

Proteins: Structure, Function and Genetics

Volumn 31, Issue 3, 1998, Pages 320-333

  Jelsch, Christian ^a,b   Longhi, Sonia ^a   Cambillau, Christian ^a  

^a Centre National de la Recherche Scientifique   (France)

^b Nancy University CNRS   (France)

Author keywords

Crystal polymorphism; Cutinase; Electrostatic and hydrophobic interactions; Hydrophobicity; Packing contacts; Protein accessible surface

Indexed keywords

CUTINASE; FUNGAL PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ALGORITHMS; BINDING SITES; CARBOXYLIC ESTER HYDROLASES; CHEMISTRY, PHYSICAL; CRYSTALLIZATION; ELECTROSTATICS; FUNGAL PROTEINS; FUSARIUM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; SOLVENTS; SURFACE PROPERTIES;

EID: 0032525183     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980515)31:3<320::AID-PROT8>3.0.CO;2-M     Document Type: Article

References (45)

1. Kolattukudy, P.E. Cutinase from fungi and pollen. In: "Lipases." Borgstrom, B., Brockman, H. (eds.). Amsterdam: Elsevier, 1984:471-504.
2. Martinez, C., De Geus, P., Lauwereys, M., Matthyssens, G., Cambillau, C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to the solvent. Nature 356:615-618, 1992.
3. Martinez, C., De Geus, P., Stanssens, P., Lauwereys, M., Cambillau, C. Engineering cysteine mutants to obtain crystallographic phases with a cutinase from Fusarium solani pisi. Protein Eng. 6:157-165, 1993.
4. Longhi, S., Czjzek, M., Lamzin, V, Nicolas, A., Cambillau, C. Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: Stereochemical analysis. J. Mol. Biol. 268:779-799, 1997.
5. Ollis, D.L., Cheah, E., Cygler, M., et al. The α/β hydrolase fold. Prot. Eng. 5:197-211, 1992.
6. Martinez, C., Nicolas, A., van Tilbeurgh, H., et al. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33:83-89, 1994.
7. Nicolas, A., Egmond, M., Verrips, C.T., et al. Contribution of cutinase serine 42 sidechain to the stabilization of the oxyanion transition state. Biochemistry 35:398-410, 1996.
8. Longhi, S., Nicolas, A., Creveld, L., et al. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins 26:442-458, 1996.
9. Longhi, S., Mannesse, M.L.M., Verheij, H.M., et al. Crystal structure of cutinase covalently inhibited by a triglyceride analogue. Protein Sci. 6:1-12, 1997.
10. Bennett, W.S., Jr., Steitz, T.A. Structure of a complex between yeast hexokinase A and glucose: Detailed comparisons of conformation and active-site conformation with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:211-230, 1980.
11. Dixon, M.M., Nicholson, H., Shewchuk, L., Baase, W.A., Matthews, B.W. Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile → Pro. J. Mol. Biol. 227:917-933, 1992.
12. Zhang, X., Wozniak, J.A., Matthews, B.W. Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250:527-552, 1995.
13. Anderson, B.F., Baker, H.M., Norris, G.E., Rumball, S.V., Baker, E.N. Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature 344:784-787, 1990.
14. Vonrhein, C., Schlauderer, G.J., Schulz, G.E. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 3:483-490, 1995.
15. Brzozowski, A.M., Derewenda, U., Derewenda, Z.S., Dodson, G., Lawson, D., Turkenburg, J.P. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351:491-494, 1991.
16. Derewenda, U., Brzozowski, A.M., Lawson, D., Derewenda, Z.S. Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase. Biochemistry 31:1532-1541, 1992.
17. van Tilbeurg, H., Egloff, M.P., Martinez, C., Rugani, N., Verger, R., Cambillau, C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 362:814-820, 1993.
18. Egloff, M.P., Marguet, R, Buono, G., Verger, R., Cambillau, C., van Tilbeurg, H. The 2.46-Å resolution structure of the pancreatic lipase-procolipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34:2751-2762, 1995.
19. Grochulski, P., Bouthillier, F., Kazlauskas, R.J., et al. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry 33:3494-3500, 1994.
20. Phillips, G.N., Jr. Comparison of the dynamics of myoglobin in different crystal forms. Biophys. J. 57:381-383, 1990.
21. Badger, J. Plexibility in crystalline insulin. Biophys. J. 61:816-819, 1992.
22. Mittl, P.R.E., Berry, A., Scrutton, N.S., Perham, R.N., Schultz, G.E. A designed mutant of the enzyme glutathione reductase shortens the crystallization time by a factor of forty. Acta Cryst. D50:228-231, 1994.
23. Heinz, D.W., Matthews, B.W. Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking. Prot. Eng. 7:301-307, 1994
24. Crosio, M.P., Janin, J., Jullien, M. Crystal packing in six crystal forms of pancreatic ribonuclease. J. Mol. Biol. 228:243-251, 1992.
25. Abergel, C., Martinez, C., Fontecilla-Camps, J., Cambillau, C., De Geus, P., Lauwereys, M. Crystallization and preliminary X-ray study of a recombinant cutinase from Fusarium solani pisi. J. Mol. Biol. 215:215-216, 1990.
26. Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., et al. The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 112:535-542, 1977.
27. Lee, B., Richards, RM. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55:379-400, 1971.
28. Brünger, A.T. "X-Plor version 3.1 manual." New Haven: Yale University, 1993.
29. Roussel, A., Cambillau, C. In: "Silicon Graphics Geometry Partners Directory." Mountain View, CA: Silicon Graphics, 1991:86.
30. Burley, S.K., Petsko, G.A. Weakly polar interactions in proteins. Adv. Prot. Chem. 39:125-189, 1988.
31. Hunter, C.A., Singh, J., Thornton, J.M. Pi-pi interactions: The geometry and energetics of phenylalanine-phenylalanine interactions in proteins. J. Mol. Biol. 218:837-846, 1991.
32. Matthews, B.M. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
33. Miller, S., Janin, J., Lesk, A.M., Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol. 196:641-656, 1987.
34. Takahashi, T., Endo, S., Nagayama, K. Stabilization of protein crystals by electrostatic interactions as revealed by a numerical approach. J. Mol. Biol. 234:421-432, 1993.
35. Honig, B., Nicholls, A. Classical electrostatics in biology and chemistry. Science 268:1144-1149, 1995.
36. Lawson, D.M., Artymiuk, P.J., Yewdall, S.J., et al. Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 349:541-544, 1991.
37. Takeda, S., Yoshimura, H., Endo, S., Takahashi, T., Nagayama, K. Control of crystal forms of apoferritin by site-directed mutagenesis. Proteins 23:548-556, 1995.
38. Ghosh, D., Wawrzak, Z., Pletnev, V.Z., et al. Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase. Structure 3:279-288, 1995.
39. Grochulski, P., Li, Y., Schrag, J.D., et al. Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 268:12843-12847, 1993.
40. Cambillau, C., Longhi, S., Nicolas, A., Martinez, C. Acyl glycerol hydrolases: Inhibitors, interface and catalysis. Curr. Opinion Struct. Biol. 6:449-455, 1996.
41. Jenkins, T.M., Hickman, A.B., Dyda, F., Ghirlando, R., Davies, D.R., Craigie, T.R. Catalytic domain of HIV-1 integrase: Identification of a soluble mutant by systematic replacement of hydrophobic residues. Proc. Natl. Sci. Acad. U.S.A. 92:6057-6061, 1995.
42. Janin, J., Chothia, C. The structure of protein-protein recognition sites. J. Biol. Chem. 265:16027-16030, 1990.
43. Janin, J., Miller, S., Chothia, C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204:155-164, 1988.
44. Janin, J., Rodier, F. Protein-protein interaction at crystal contacts. Proteins 23:580-587, 1996.
45. Salemme, F.R., Genieser, L., Finzel, B.C., Humer, R.M., Wendoloski, J.J. Molecular factors stabilizing protein crystals. J. Crystal Growth. 90:273-282, 1988.