The Crystal Structure of Pichia pastoris Lysyl Oxidase

Biochemistry

Volumn 42, Issue 51, 2003, Pages 15148-15157

  Duff, Anthony P ^a   Cohen, Aina E ^b   Ellis, Paul J ^b   Kuchar, Jason A ^c,d   Langley, David B ^a   Shepard, Eric M ^c   Dooley, David M ^c   Freeman, Hans C ^a   Guss, J Mitchell ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c MONTANA STATE UNIVERSITY   (United States)

^d UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER COMPOUNDS; CRYSTAL STRUCTURE; POLYPEPTIDES; YEAST;

TOPAQUINONE COFACTORS (TPQ);

ENZYMES;

COPPER AMINE OXIDASE; LYSINE; OXIDOREDUCTASE; POLYPEPTIDE; PROTEIN LYSINE 6 OXIDASE; QUININE; TROPOELASTIN; TYROSINE; UNCLASSIFIED DRUG;

AORTA; ARTICLE; ATOM; CATALYSIS; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; OXIDATION; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN PROCESSING;

AMINE OXIDASE (COPPER-CONTAINING); ANIMALS; ARTHROBACTER; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIHYDROXYPHENYLALANINE; DIMERIZATION; FUNGAL PROTEINS; HUMANS; MODELS, MOLECULAR; PEAS; PICHIA; PROTEIN SUBUNITS; PROTEIN-LYSINE 6-OXIDASE; SUBSTRATE SPECIFICITY;

BOVINAE; CINCHONA PUBESCENS; MAMMALIA; PICHIA PASTORIS;

EID: 0346333359     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035338v     Document Type: Article

References (45)

1. Binda, C., Mattevi, A., and Edmondson, D. E. (2002) Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. J. Biol. Chem. 277, 23973-6.
2. Kagan, H. M. (1994) Lysyl oxidase: mechanism, regulation and relationship to liver fibrosis. Pathol. Res. Pract. 190, 910-9.
3. Wang, S. X., Mure, M., Medzihradszky, K. F., Burlingame, A. L., Brown, D. E., Dooley, D. M., Smith, A. J., Kagan, H. M., and Klinman, J. P. (1996) A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science 273, 1078-84.
4. Kim, M., Okajima, T., Kishishita, S., Yoshimura, M., Kawamori, A., Tanizawa, K., and Yamaguchi, H. (2002) X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase. Nat. Struct. Biol. 9, 591-6.
5. Tanizawa, K. (1995) Biogenesis of novel quinone coenzymes. J. Biochem. (Tokyo) 118, 671-8.
6. Cai, D., and Klinman, J. P. (1994) Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J. Biol. Chem. 269, 32039-42.
7. Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y., and Tanizawa, K. (1994) Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351, 360-4.
8. Ruggiero, C. E., Smith, J. A., Tanizawa, K., and Dooley, D. M. (1997) Mechanistic studies of topa quinone biogenesis in phenylethylamine oxidase. Biochemistry 36, 1953-9.
9. Dooley, D. M. (1999) Structure and biogenesis of topaquinone and related cofactors. J. Biol. Inorg. Chem. 4, 1-11.
10. Wilmot, C. M., Hajdu, J., McPherson, M. J., Knowles, P. F., and Phillips, S. E. (1999) Visualization of dioxygen bound to copper during enzyme catalysis. Science 286, 1724-8.
11. Wilmot, C. M., Murray, J. M., Alton, G., Parsons, M. R., Convery, M. A., Blakeley, V., Comer, A. S., Palcic, M. M., Knowles, P. F., McPherson, M. J., and Phillips, S. E. (1997) Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Biochemistry 36, 1608-20.
12. Wilce, M. C. J., Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., McIntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H. (1997) Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo- and apo-forms: implications for the biogenesis of topa quinone. Biochemistry 36, 16116-33.
13. Mills, S. A., and Klinman, J. P. (2000) Evidence Against Reduction of Cu2+ to Cu+ during Dioxygen Activation in a Copper Amine Oxidase from Yeast. J. Am. Chem. Soc. 122, 9897-904.
14. Mills, S. A., Goto, Y., Su, Q., Plastino, J., and Klinman, J. P. (2002) Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha. Biochemistry 41, 10577-84.
15. Elmore, B. O., Bollinger, J. A., and Dooley, D. M. (2002) Human kidney diamine oxidase: heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. 7, 565-79.
16. McIntire, W. S., and Hartmann, C. (1993) Copper-containing amine oxidases in Principles and Applications of Quinoproteins (Davidson, V. L., Ed.) pp 97-171, Marcel Dekker, Inc, New York.
17. Sebela, M., Frebort, I., Petrivalsky, M., and Pec, P. (2002) Copper/ topa quinone-containing amine oxidases - Recent research developments. Stud. Nat. Prod. Chem. 26, 1259-99.
18. Salmi, M., Hellman, J., and Jalkanen, S. (1998) The role of two distinct endothelial molecules, vascular adhesion protein-1 and peripheral lymph node addressin, in the binding of lymphocyte subsets to human lymph nodes. J. Immunol. 160, 5629-36.
19. Yu, P. H., Wright, S., Fan, E. H., Lun, Z. R., and Gubisne-Harberle, D. (2003) Physiological and pathological implications of semicarbazide-sensitive amine oxidase. Biochim. Biophys. Acta 1647, 193-9.
20. Parsons, M. R., Convery, M. A., Wilmot, C. M., Yadav, K. D., Blakeley, V., Comer, A. S., Phillips, S. E., McPherson, M. J., and Knowles, P. F. (1995) Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure 3, 1171-84.
21. Kumar, V., Dooley, D. M., Freeman, H. C., Guss, J. M., Harvey, I., McGuirl, M. A., Wilce, M. C. J., and Zubak, V. M. (1996) Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 Å resolution. Structure 4, 943-55.
22. Li, R., Klinman, J. P., and Mathews, F. S. (1998) Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation. Structure 6, 293-307.
23. Dove, J. E., and Klinman, J. P. (2001) Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase. Adv. Prot. Chem. 58, 141-74.
24. Dawkes, H. C., and Phillips, S. E. (2001) Copper amine oxidase: cunning cofactor and controversial copper. Curr. Opin. Struct. Biol. 11, 666-73.
25. Halcrow, M., Phillips, S., and Knowles, P. (2000) Amine oxidases and galactose oxidase. Subcell. Biochem. 35, 183-231.
26. Green, J., Haywood, G. W., and Large, P. J. (1983) Serological differences between the multiple amine oxidases of yeasts and comparison of the specificities of the purified enzymes from Candida utilis and Pichia pastoris. Biochem. J. 211, 481-93.
27. Tur, S. S., and Lerch, K. (1988) Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase. FEBS Lett. 238, 74-6.
28. Kuchar, J. A., and Dooley, D. M. (2001) Cloning, sequence analysis, and characterization of the 'Lysyl Oxidase' from Pichia pastoris. J. Inorg. Biochem. 83, 193-204.
29. Dove, J. E., Smith, A. J., Kuchar, J., Brown, D. E., Dooley, D. M., and Klinman, J. P. (1996) Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. FEBS Lett. 398, 231-4.
30. Lee, M., Willingham, K., Langley, D., Maher, M. J., Cohen, A. E., Ellis, P. J., Kuchar, J. A., Dooley, D. M., Freeman, H. C., and Guss, J. M. (2002) Crystallization of Pichia pastoris lysyl oxidase. Acta Crystallogr. D58, 2177-9.
31. Navaza, J. (1994) AMoRe: an Automated Package for Molecular Replacement. Acta Crystallogr. D55, 157-63.
32. Matthews, B. W. (1968) Solvent Content of Protein Crystals. J. Mol. Biol. 33, 491-7.
33. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J. (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-10.
34. Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grossekunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography and NMR system - a new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905-21.
35. Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-9.
36. Cowtan, K. (1994) An automated procedure for phase improvement by density modification, Joint CCP4 and ESF-EA CBM Newsletter on Protein Crystallography 31, 34-8.
37. Perrakis, A., Harkiolaki, M., Wilson, K. S., and Lamzin, V. S. (2001) ARP/wARP and molecular replacement. Acta Crystallogr. D57, 1445-50.
38. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53, 240-55.
39. CCP4. (1994) Collaborative Computational Project no. 4, Acta Crystallogr. D50, 760-3.
40. Bedell-Hogan, D., Trackman, P., Abrams, W., Rosenbloom, J., and Kagan, H. (1993) Oxidation, cross-linking, and insolubilization of recombinant tropoelastin by purified lysyl oxidase. J. Biol. Chem. 268, 10345-50.
41. Kuchar, J. A. (2001) Cloning, sequence analysis, and characterization of the 'lysyl oxidase' from Pichia pastoris, Ph.D. Thesis, Montana State University.
42. Kagan, H. M., and Cai, P. (1995) Isolation of active site peptides of lysyl oxidase. Methods Enzymol. 258, 122-32.
43. Kleywegt, G. J., and Jones, T. A. (1994) Detection, Delineation, Measurement and Display of Cavities in Macromolecular Structures. Acta Crystallogr. D50, 178-85.
44. Delano, W. L. (2002) Delano Scientific, San Carlos, CA.
45. Cruickshank, D. W. J. (1999) Remarks about protein structure precision. Acta Crystallogr. D55, 583-601.