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Volumn 46, Issue 1, 2006, Pages 17-26

Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-Å resolution

Author keywords

aminoadipate pathway; ARP wARP; Automated model building; Crystal structure; Lysine biosynthesis; Molecular replacement; NADPH; Phaser; Saccharopine reductase

Indexed keywords

HISTIDINE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SACCHAROPINE DEHYDROGENASE; SACCHAROPINE DEHYDROGENASE (NADP, L GLUTAMATE FORMING); SACCHAROPINE DEHYDROGENASE (NADP, L-GLUTAMATE-FORMING);

EID: 33748306053     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:46:1:17     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0034141893 scopus 로고    scopus 로고
    • Lysine biosynthesis and metabolism in fungi
    • Zabriskie, T. M., and Jackson, M. D. (2000) Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17, 85-97.
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 85-97
    • Zabriskie, T.M.1    Jackson, M.D.2
  • 2
    • 0028830864 scopus 로고
    • Having a blast: Exploring the pathogenicity of Magnaporthe grisea
    • Talbot, N. J. (1995) Having a blast: exploring the pathogenicity of Magnaporthe grisea. Trends Microbiol. 3, 9-16.
    • (1995) Trends Microbiol. , vol.3 , pp. 9-16
    • Talbot, N.J.1
  • 3
    • 0034435381 scopus 로고    scopus 로고
    • Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis
    • Johansson, E., Steffens, J. J., Lindqvist, Y., and Schneider, G. (2000) Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis. Struct. Fold Des. 8, 1037-1047.
    • (2000) Struct. Fold Des. , vol.8 , pp. 1037-1047
    • Johansson, E.1    Steffens, J.J.2    Lindqvist, Y.3    Schneider, G.4
  • 4
    • 0021906426 scopus 로고
    • Alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes
    • Bhattacharjee, J. K. (1985) alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes. Crit. Rev. Microbiol. 12, 131-151.
    • (1985) Crit. Rev. Microbiol. , vol.12 , pp. 131-151
    • Bhattacharjee, J.K.1
  • 5
    • 77957016095 scopus 로고
    • Lysine biosynthesis (yeast)
    • Broquist, H. P. (1971) Lysine biosynthesis (yeast). Methods Enzymol. 17B, 112-129.
    • (1971) Methods Enzymol. , vol.17 B , pp. 112-129
    • Broquist, H.P.1
  • 6
    • 0000773895 scopus 로고
    • Regulation of amino acid and nucleotide synthesis in yeast
    • (Strathern, J. N., Jones, E. W., and Broach, J. R., eds.) Cold Spring Harbor Laboratory, Cold spring Harbor, NY
    • Jones, E. W. and Fink, G. R. (1982) Regulation of amino acid and nucleotide synthesis in yeast, in Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Regulation (Strathern, J. N., Jones, E. W., and Broach, J. R., eds.) Cold Spring Harbor Laboratory, Cold spring Harbor, NY, pp. 181-299.
    • (1982) Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Regulation , pp. 181-299
    • Jones, E.W.1    Fink, G.R.2
  • 7
    • 33748290014 scopus 로고    scopus 로고
    • The α-aminoadipate pathway for lysine biosynthesis in fungi
    • Xu, H., Andi, B., Qian, J., West, A. H., and Cook, P. F. (2006) The α-aminoadipate pathway for lysine biosynthesis in fungi. Cell Biochem. Biophys. 46, 43-64.
    • (2006) Cell Biochem. Biophys. , vol.46 , pp. 43-64
    • Xu, H.1    Andi, B.2    Qian, J.3    West, A.H.4    Cook, P.F.5
  • 8
    • 0023156845 scopus 로고
    • Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway
    • Storts, D. R. and Bhattacharjee, J. K. (1987) Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway. J. Bacteriol. 169, 416-418.
    • (1987) J. Bacteriol. , vol.169 , pp. 416-418
    • Storts, D.R.1    Bhattacharjee, J.K.2
  • 9
    • 0014027810 scopus 로고
    • Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase
    • Jones, E. E. and Broquist, H. P. (1966) Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase. J. Biol. Chem. 241, 3430-3434.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3430-3434
    • Jones, E.E.1    Broquist, H.P.2
  • 10
    • 0002974535 scopus 로고
    • Evolution of α-aminoadipate pathway for the synthesis of lysine in fungi
    • (Mortlock, R. P., ed.), CRC, Boca Raton, FL
    • Bhattacharjee, J. K. (1992) Evolution of α-aminoadipate pathway for the synthesis of lysine in fungi, in Evolution of Metabolic Function (Mortlock, R. P., ed.), CRC, Boca Raton, FL, pp. 47-80.
    • (1992) Evolution of Metabolic Function , pp. 47-80
    • Bhattacharjee, J.K.1
  • 12
    • 1542563485 scopus 로고
    • Evolutionary and structural relationship among dehydrogenases
    • Rossmann, M. G., Liljas, A., Branden, C. I., and Banaszak, L. J. (1975) Evolutionary and structural relationship among dehydrogenases. Enzymes 11, 51-102.
    • (1975) Enzymes , vol.11 , pp. 51-102
    • Rossmann, M.G.1    Liljas, A.2    Branden, C.I.3    Banaszak, L.J.4
  • 13
    • 0037246767 scopus 로고    scopus 로고
    • The CATH database: An extended protein family resource for structural and functional genomics
    • Pearl, F. M., Bennett, C. F., Bray, J. E., et al. (2003) The CATH database: an extended protein family resource for structural and functional genomics. Nucleic Acids Res. 31, 452-455.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 452-455
    • Pearl, F.M.1    Bennett, C.F.2    Bray, J.E.3
  • 14
    • 0023156845 scopus 로고
    • Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway
    • Storts, D. R. and Bhattacharjee, J. K. (1987) Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway. J. Bacteriol. 169, 416-418.
    • (1987) J. Bacteriol. , vol.169 , pp. 416-418
    • Storts, D.R.1    Bhattacharjee, J.K.2
  • 15
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55, 1718-1725.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 16
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57, 1373-1382.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 20
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 23
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 24
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 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.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.