Structural Basis of Phospholipase Activity of Staphylococcus hyicus lipase

Journal of Molecular Biology

Volumn 371, Issue 2, 2007, Pages 447-456

  Tiesinga, Jan J W ^a   Pouderoyen, Gertie van ^a   Nardini, Marco ^a   Ransac, Stéphane ^a   Dijkstra, Bauke W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

alpha beta hydrolase fold; crystal structure; phospholipase; Staphylococcus hyicus lipase; substrate specificity

Indexed keywords

PHOSPHOLIPASE; PHOSPHOLIPID; TRIACYLGLYCEROL LIPASE;

ARTICLE; CATALYST; CRYSTAL STRUCTURE; ELECTRICITY; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; STAPHYLOCOCCUS HYICUS;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS HYICUS;

EID: 34447293088     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.041     Document Type: Article

References (45)

1. Jaeger K.E., Dijkstra B.W., and Reetz M.T. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Microbiol. 53 (1999) 315-351
2. Götz F., Verheij H.M., and Rosenstein R. Staphylococcal lipases: molecular characterisation, secretion, and processing. Chem. Phys. Lipids 93 (1998) 15-25
3. Rosenstein R., and Götz F. Staphylococcal lipases: biochemical and molecular characterization. Biochimie 82 (2000) 1005-1014
4. Gupta R., Gupta N., and Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Appl. Microbiol. Biotechnol. 64 (2004) 763-781
5. Sarda L., and Desnuelle P. Actions of pancreatic lipase on esters in emulsions. Biochim. Biophys. Acta 30 (1958) 513-521
6. Derewenda Z.S., and Sharp A.M. News from the interface: the molecular structures of triacylglyceride lipases. Trends Biochem. Sci. 18 (1993) 20-25
7. Secundo F., Carrea G., Tarabiono C., Gatti-Lafranconi P., Brocca S., Lotti M., et al. The lid is a structural and functional determinant of lipase activity and selectivity. J. Mol. Cat. B Enzym. 39 (2006) 166-170
8. Arpigny J.L., and Jaeger K.E. Bacterial lipolytic enzymes: classification and properties. Biochem. J. 343 (1999) 177-183
9. Nardini M., and Dijkstra B.W. α/β Hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9 (1999) 732-737
10. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., et al. The α/β hydrolase fold. Protein Eng. 5 (1992) 197-211
11. van Oort M.G., Deveer A.M.T.J., Dijkman R., Leuveling Tjeenk M., Verheij H.M., de Haas G.H., et al. Purification and substrate specificity of Staphylococcus hyicus lipase. Biochemistry 28 (1989) 9278-9285
12. Simons J.W.F.A., Götz F., Egmond M.R., and Verheij H.M. Biochemical properties of staphylococcal (phospho)lipases. Chem. Phys. Lipids 93 (1998) 27-37
13. Jaeger K.E., and Eggert T. Lipases for biotechnology. Curr. Opin. Biotechnol. 13 (2002) 390-397
14. Leuveling Tjeenk M., Bulsink Y.B.M., Slotboom A.J., Verheij H.M., de Haas G.H., Demleitner G., and Götz F. Inactivation of Staphylococcus hyicus lipase by hexadecylsulfonyl fluoride: evidence for an active site serine. Protein Eng. 7 (1994) 579-583
15. Jäger S., Demleitner G., and Götz F. Lipase of Staphylococcus hyicus: analysis of the catalytic triad by site-directed mutagenesis. FEMS Microbiol. Letters 100 (1992) 249-254
16. Boots J.W.P., van Dongen W.D., Verheij H.M., de Haas G.H., Haverkamp J., and Slotboom A.J. Identification of the active site histidine in Staphylococcus hyicus lipase using chemical modification and mass spectrometry. Biochim. Biophys. Acta 1248 (1995) 27-34
17. van Kampen M.D., Simons J.W.F.A., Dekker N., Egmond M.R., and Verheij H.M. The phospholipase activity of Staphylococcus hyicus lipase strongly depends on a single Ser to Val mutation. Chem. Phys. Lipids 93 (1998) 39-45
18. van Kampen M.D., Verheij H.M., and Egmond M.R. Modifying the substrate specificity of staphylococcal lipases. Biochemistry 38 (1999) 9524-9532
19. Simons J.W.F.A., van Kampen M.D., Ubarretxena-Belandia I., Cox R.C., Alves dos Santos C.M., Egmond M.R., and Verheij H.M. Identification of a calcium binding site in Staphylococcus hyicus lipase: generation of calcium-independent variants. Biochemistry 38 (1999) 2-10
20. Lang D.A., Mannesse M.L.M., de Haas G.H., Verheij H.M., and Dijkstra B.W. Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. Eur. J. Biochem. 254 (1998) 333-340
21. Simons J.W.F.A., Boots J.W., Kats M.P., Slotboom A.J., Egmond M.R., and Verheij H.M. Dissecting the catalytic mechanism of staphylococcal lipases using carbamate substrates: chain length selectivity, interfacial activation, and cofactor dependence. Biochemistry 36 (1997) 14539-14550
22. Simons J.W.F.A., Adams H., Cox R.C., Dekker N., Götz F., Slotboom A.J., and Verheij H.M. The lipase from Staphylococcus aureus. Expression in Escherichia coli, large-scale purification and comparison of substrate specificity to Staphylococcus hyicus lipase. Eur. J. Biochem. 242 (1996) 760-769
23. Ransac S., Blaauw M., Dijkstra B.W., Slotboom A.T., Boots J.W.P., and Verheij H.M. Crystallization and preliminary X-ray analysis of a lipase from Staphylococcus hyicus. J. Struct. Biol. 114 (1995) 153-155
24. Jeong S.T., Kim H.K., Kim S.J., Chi S.W., Pan J.G., Oh T.K., and Ryu S.E. Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase. J. Biol. Chem. 277 (2002) 17041-17047
25. Tyndall J.D., Sinchaikul S., Fothergill-Gilmore L.A., Taylor P., and Walkinshaw M.D. Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1. J. Mol. Biol. 323 (2002) 859-869
26. Götz F., Popp F., Korn E., and Schleifer K.H. Complete nucleotide sequence of the lipase gene from Staphylococcus hyicus cloned in Staphylococcus carnosus. Nucl. Acids Res. 13 (1985) 5895-5906
27. Suhre K., and Sanejouand Y.H. On the potential of normal-mode analysis for solving difficult molecular-replacement problems. Acta Crystallog. sect. D 60 (2004) 796-799
28. Kim K.K., Song H.K., Shin D.H., Hwang K.Y., and Suh S.W. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure 5 (1997) 173-185
29. van Kampen M.D., Dekker N., Egmond M.R., and Verheij H.M. Substrate specificity of Staphylococcus hyicus lipase and Staphylococcus aureus lipase as studied by in vivo chimeragenesis. Biochemistry 37 (1998) 3459-3466
30. Simons J.W.F.A., van Kampen M.D., Riel S., Götz F., Egmond M.R., and Verheij H.M. Cloning, purification and characterisation of the lipase from Staphylococcus epidermidis - comparison of the substrate selectivity with those of other microbial lipases. Eur. J. Biochem. 253 (1998) 675-683
31. van Kampen M.D., Rosenstein R., Götz F., and Egmond M.R. Cloning, purification and characterisation of Staphylococcus warneri lipase 2. Biochim. Biophys. Acta 1544 (2001) 229-241
32. Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucl. Acids Res. 31 (2003) 3381-3385
33. 2 complexed with a substrate-derived inhibitor. Nature 347 (1990) 689-691
34. 2 from inflammatory exudate. Science 254 (1991) 1007-1010
35. Nardini M., Lang D.A., Liebeton K., Jaeger K.E., and Dijkstra B.W. Crystal structure of Pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases. J. Biol. Chem. 275 (2000) 31219-31225
36. Choi W.C., Kim M.H., Ro H.S., Ryu S.R., Oh T.K., and Lee J.K. Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability. FEBS Letters 579 (2005) 3461-3466
37. Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallog. sect. D 62 (2006) 48-57
38. Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
39. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
40. Terwilliger T.C. Map-likelihood phasing. Acta Crystallog. sect D 57 (2001) 1763-1775
41. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
42. Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
43. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
44. Schüttelkopf A.W., and van Aalten D.M.F. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallog. sect. D 60 (2004) 1355-1363
45. Gouet P., Courcelle E., Stuart D.I., and Métoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308