Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli

Biochemistry

Volumn 44, Issue 24, 2005, Pages 8620-8626

  Claus, Michael T ^a   Zocher, Georg E ^a   Maier, Thomas H P ^b   Schulz, Georg E ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b WACKER CHEMIE AG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; PLANTS (BOTANY); POLYPEPTIDES; SUBSTRATES;

BUILDING BLOCKS; L-CYSTEINE; MUTANTS; STRUCTURAL SUPERPOSITIONS;

ENZYMES;

CYSTEINE SYNTHASE; CYSTEINE SYNTHASE K; CYSTEINE SYNTHASE M; ISOENZYME; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MATHEMATICAL MODEL; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; REACTION ANALYSIS;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; CYSTEINE SYNTHASE; DIMERIZATION; ESCHERICHIA COLI; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 20544435016     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050485+     Document Type: Article

References (39)

1. Kredich, N. M. (1971) Regulation of L-cysteine biosynthesis in Salmonella typhimurium, J. Biol. Chem. 246, 3474-3484.
2. Cooper, A. J. L. (1983) Biochemistry of sulfur-containing amino acids, Annu. Rev. Blochem. 52, 187-222.
3. Kredich, N. M. (1996) Biosynthesis of cysteine, in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhard, F. C., Ed.) Vol. 2, pp 514-527, ASM Press, Washington, DC.
4. Borup, B., and Ferry, J. G. (2000) Cysteine biosynthesis in the Archaea: Methanosarcina thermophila utilizes O-acetylserine sulfhydrylase, FEMS Microbiol. Lett. 189, 205-210.
5. Mino, K., and Ishikawa, K. (2003) Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J. Bacteriol. 185, 2277-2284.
6. Wirtz, M., Droux, M., and Hell, R. (2004) O-acetylserine (thiol) lyase: An enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsls thaliana, J. Exp. Bot. 55, 1785-1798.
7. Cook, P. F., and Wedding, R. T. (1978) Cysteine synthetase from Salmonella typhimiirium LT-2, J. Biol. Chem. 253, 7874-7879.
8. Burkhard, P., Rao, G. S. J., Hohenester, E., Schnackerz, K. D., Cook, P. F., and Jansonius, J. N. (1998) Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium, J. Mol. Biol. 283, 121-133.
9. Tai, C. H., Burkhard, P., Gani, D., Jenn, T., Johnson, C., and Cook, P. F. (2001) Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase, Biochemistry 40, 7446-7452.
10. Tai, C. H., and Cook, P. F. (2001) Pyridoxal 5′-phosphate-dependent α,β-elimination reactions: mechanism of O-acetylserine sulfhydrylase, Acc. Chem. Res. 34, 49-59.
11. Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Minier, D. E., and Cook, P. F. (1993) Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants, Biochemistry 32, 6433-6442.
12. Maier, T. H. P. (2003) Semisynthetic production of unnatural L-α-amino acids by metabolic engineering of the cysteine biosynthetic pathway, Nat. Biotechnol. 21, 422-427.
13. Watkins, K. J. (2001) Peptides: A boom in the making, Chem. Eng. News, 11-15 (January 8).
14. Schnackerz, K. D., and Cook, P. F. (1995) Resolution of pyridoxal 5′-phosphate from O-acetylserine suifhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site, Arch. Biochem. Biophys. 324, 71-77.
15. Hidalgo, C., Sevilla, J. M., Pineda, T., and Blazquez, M. (1994) Enolimine and geminaldiamine forms in the reaction of pyridoxal phosphate with ethylenediamine. An electrochemical and spectroscopic contribution, J. Phys. Org. Chem. 7, 227-233.
16. Doublie, S. (1997) Preparation of selenomethionyl proteins for phase determination, Methods Enzymol. 276, 523-530.
17. Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, J. Appl. Crystallogr. 26, 795-800.
18. Navaza, J. (1994) AMORE: an automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
19. Hendrickson, W. A., Horton, J. R., and Le Master, D. M. (1990) Selenomethionyl proteins produced for analysis by multiwave-length anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure, EMBO J. 9, 1665-1672.
20. Schneider, T. R., and Sheldrick, G. M. (2002) Substructure solution with SHELXD, Acta Crystallogr. D58, 1772-1779.
21. Sheldrick, G. M. (2002) Macromolecular phasing with SHELXE, Z. Kristallogr. 217, 644-650.
22. de La Fortelle, E., and Bricogne, G. (1997) Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods, Methods Enzymol. 276, 472-494.
23. CCP4, Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
24. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum likelihood method, Acta Crystallogr. D53, 240-255.
25. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N. S., et al. (1998) Crystallography and NMR system (CNS): A new software system for macromolecular structure determination, Acta Crystallogr. D54, 905-921.
26. Perrakis, A., Sixma, T. K., Wilson, K. S., and Lamzin, V. S. (1997) wARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models, Acta Crystallogr. D53, 448-455.
27. Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
28. Terwilliger, T. C. (2002) Automated main-chain model-building by template-matching and iterative fragment extension, Acta Crystallogr. D59, 34-44.
29. Yeates, T. O. (1997) Detecting and overcoming crystal twinning, Methods Enzymol. 276, 344-358.
30. Sheldrick, G. M. (1998) SHELX: Applications to macromolecules, in Direct methods for solving macromolecular structures (Fortier, S., Ed.) pp 401-411, Kluwer, Dordrecht, The Netherlands.
31. Hubbard, S. J., and Thornton, J. M. (1993) NACCESS computer program, Department of Biochemistry and Molecular Biology, University College, London, U.K.
32. Fenn, T. D., Ringe, D., and Petsko, G. A. (2003) POVScript+: a program for model and data visualization using persistence of vision ray-tracing, J. Appl. Crystallogr. 36, 944-947.
33. Burkhard, P., Tai, C.-H., Ristoph, C. M., Cook, P. F., and Jansonius, J. N. (1999) Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium, J. Mol. Biol. 291, 941-953.
34. Burkhard, P., Tai, C.-H., Jansonius, J. N., and Cook, P. F. (2000) Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: Structure of the enzyme with chloride bound, J. Mol. Biol. 303, 279-286.
35. Heine, A., Canaves, J. M., von Delft, F., Brinen, L. S., Dai, X., Deacon A. M., Elsliger, M. A., Eshaghi, S., Floyd, R., Godzik, A., Grittini, C., Grzechnik, S. K., Guda, C., Jaroszewski, L., Karlak, C., Klock, H. E., Koesema, E., Kovarik, J. S., Kreusch, A., Kuhn, P., Lesley, S. A., McMullan, D., McPhillips, T. M., Miller, M. A., Miller, M. D., Morse, A., Moy, K., Ouyang, J., Page, R., Robb, A., Rodrigues, K., Schwarzenbacher, R., Selby, T. L., Spraggon, G., Stevens, R. C., van den Bedem, H., Velasquez, J., Vincent, J., Wang, X., West, B., Wolf, G., Hodgson, K. O., Wooley, J., and Wilson, I. A. (2004) Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 Å resolution, Proteins: Struct., Funct., Genet. 56, 387-391.
36. Schulz, G. E. (1992) Binding of nucleotides by proteins, Curr. Opin. Struct. Biol. 2, 61-67.
37. Kaldor, S. W., Kalish, V. J., Davies II, J. F., Shetty, B. V., Fritz, J. E., Appelt, K., Burgess, J. A., Campanale, K. M., Chirgadze, N. Y., Clawson, D. K., Dressmann, B. A., Hatch, S. D., Khalil, D. A., Kosa, M. B., Lubbehusen, P. P., Muesing, M. A., Patrick, A. K., Reich, S. H., Su, K. S., and Tatlock, J. H., (1997) Viracept (Nelfinavir Mesylate, AG1343): a potent, orally bioavailable inhibitor of HIV-1 protease, J. Med. Chem. 40, 3979-3985.
38. Kantardjieff, K. A., and Rupp, B. (2003) Matthews coefficient probabilities: improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals, Protein Sci. 12, 1865-1871.
39. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.