메뉴 건너뛰기




Volumn 4, Issue 7, 1996, Pages 801-810

Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: Evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6- phosphate synthase

Author keywords

catalytic mechanism; crystal structure; glucosamine 6 phosphate synthase; glutaminase domain; glutamine amidotransferase

Indexed keywords


EID: 0030586024     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00087-1     Document Type: Article
Times cited : (145)

References (29)
  • 2
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • Tesmer, J.J.G., Klem, T.J., Deras, M.L., Davisson, V.J. & Smith, Jl. (1996). The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat. Struct. Biol. 3, 74-86.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 74-86
    • Tesmer, J.J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.5
  • 3
    • 0020478925 scopus 로고
    • Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase
    • Tso, J.Y., Zalkin, H., van Cleemput, M., Yanofsky, C. & Smith, J.M. (1982). Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 257, 3525-3531.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3525-3531
    • Tso, J.Y.1    Zalkin, H.2    Van Cleemput, M.3    Yanofsky, C.4    Smith, J.M.5
  • 4
    • 0023280276 scopus 로고
    • Glucosamine synthetase from Escherichia coli: Purification, properties, and glutamine-utilizing site location
    • Badet, B., Vermoote, P., Haumont, P.-Y., Lederer, F. & Le Goffic, F. (1987). Glucosamine synthetase from Escherichia coli: purification, properties, and glutamine-utilizing site location. Biochemistry 26, 1940-1948.
    • (1987) Biochemistry , vol.26 , pp. 1940-1948
    • Badet, B.1    Vermoote, P.2    Haumont, P.-Y.3    Lederer, F.4    Le Goffic, F.5
  • 5
    • 0018908432 scopus 로고
    • Genetic and biochemical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli
    • Humbert, R. & Simoni, R.D. (1980). Genetic and biochemical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli. J. Bacteriol. 142, 212-220.
    • (1980) J. Bacteriol. , vol.142 , pp. 212-220
    • Humbert, R.1    Simoni, R.D.2
  • 6
    • 0015523879 scopus 로고
    • Glutamate synthase from Escherichia coli W, an iron-sulfide flavoprotein
    • Miller, R.E. & Stadtman, E.R. (1972). Glutamate synthase from Escherichia coli W, an iron-sulfide flavoprotein. J. Biol. Chem. 247, 7407-7419.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7407-7419
    • Miller, R.E.1    Stadtman, E.R.2
  • 7
    • 0024433662 scopus 로고
    • A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases
    • Mei, B. & Zalkin, H. (1989). A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases. J. Biol. Chem. 264, 16613-16619.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16613-16619
    • Mei, B.1    Zalkin, H.2
  • 8
    • 0026501816 scopus 로고
    • Chemical modification of glucosamine 6-phosphate synthase by diethyl pyrocarbonate: Evidence of histidine requirement for enzymatic activity
    • Badet-Denisot, M.-A. & Badet, B. (1992). Chemical modification of glucosamine 6-phosphate synthase by diethyl pyrocarbonate: evidence of histidine requirement for enzymatic activity. Arch. Biochem. Biophys. 292, 475-478.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 475-478
    • Badet-Denisot, M.-A.1    Badet, B.2
  • 9
    • 0028246266 scopus 로고
    • Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad
    • Boehlein, S.K., Richards, N.G. & Schuster, S.M. (1994). Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. J. Biol. Chem. 269, 7450-7457.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7450-7457
    • Boehlein, S.K.1    Richards, N.G.2    Schuster, S.M.3
  • 10
    • 0028762844 scopus 로고
    • Structure of the allosteric regulatory enzyme of purine biosynthesis
    • Smith, J.L., et al., & Satow, Y (1994). Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264, 1427-1433.
    • (1994) Science , vol.264 , pp. 1427-1433
    • Smith, J.L.1    Satow, Y.2
  • 11
    • 0028828360 scopus 로고
    • Structures of glutamine amidotransferases from the purine biosynthetic pathway
    • Smith, J.L. (1995). Structures of glutamine amidotransferases from the purine biosynthetic pathway. Biochem. Soc. Trans. 23, 894-898.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 894-898
    • Smith, J.L.1
  • 12
    • 0025851177 scopus 로고
    • Glucosamine 6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: Identification of the glutamine amidohydrolase and 2 R ketose/aldose isomerase-bearing domains based on their biochemical properties
    • Denisot, M.-A., Le Goffic, F. & Badet, B.(1991). Glucosamine 6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: identification of the glutamine amidohydrolase and 2 R ketose/aldose isomerase-bearing domains based on their biochemical properties. Arch. Biochem. Biophys. 288, 225-230.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 225-230
    • Denisot, M.-A.1    Le Goffic, F.2    Badet, B.3
  • 13
    • 0028117649 scopus 로고
    • Crystallization and preliminary X-ray analysis of the two domains of glucosamine 6-phosphate synthase from Escherichia coli
    • Obmolova, G., Badet-Denisot, M.-A., Badet, B. & Teplyakov, A. (1994). Crystallization and preliminary X-ray analysis of the two domains of glucosamine 6-phosphate synthase from Escherichia coli. J. Mol. Biol. 242, 703-705.
    • (1994) J. Mol. Biol. , vol.242 , pp. 703-705
    • Obmolova, G.1    Badet-Denisot, M.-A.2    Badet, B.3    Teplyakov, A.4
  • 14
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 15
    • 0025113022 scopus 로고
    • β-Turns and their distortions: A proposed new nomenclature
    • Wilmot, C.M. & Thornton, J.M. (1990). β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3, 479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 16
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan, J.A., et al., & Murzin, A.G. (1995). A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378, 416-419.
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Murzin, A.G.2
  • 17
    • 0029446407 scopus 로고
    • A sting in the (N-terminal) tail
    • Artymiuk, P.J. (1995). A sting in the (N-terminal) tail. Nat. Struct. Biol. 2, 1035-1037.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1035-1037
    • Artymiuk, P.J.1
  • 18
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • in press
    • Kim, J.H., Krahn, J.M., Tomchick, D.R., Smith, J.L. & Zalkin, H. (1996). Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem., in press.
    • (1996) J. Biol. Chem.
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 19
    • 0001083651 scopus 로고
    • Mechanistic investigations of glucosamine 6-phosphate synthase
    • Badet-Denisot, M.-A., Rene, L. & Badet, B. (1993). Mechanistic investigations of glucosamine 6-phosphate synthase. Bull. Soc. Chim. Fr. 130, 249-255.
    • (1993) Bull. Soc. Chim. Fr. , vol.130 , pp. 249-255
    • Badet-Denisot, M.-A.1    Rene, L.2    Badet, B.3
  • 20
    • 0029166093 scopus 로고
    • A stable carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase
    • Kim, J.H., Wolle, D., Haridas, K., Parry, R.J., Smith, J.L. & Zalkin, H. (1995). A stable carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 270, 17394-17399.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17394-17399
    • Kim, J.H.1    Wolle, D.2    Haridas, K.3    Parry, R.J.4    Smith, J.L.5    Zalkin, H.6
  • 21
    • 0027985441 scopus 로고
    • Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B
    • Boehlein, S.K., Richards, N.G.J., Walworth, E.S. & Schuster, S.M. (1994). Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B. J. Biol. Chem. 269, 26789-26795.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26789-26795
    • Boehlein, S.K.1    Richards, N.G.J.2    Walworth, E.S.3    Schuster, S.M.4
  • 22
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds.), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend (Sawyer, L., Isaacs, N. & Bailey, S., eds.), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: An automated package for molecular replacement. Acta Cryst. D 50, 157-163.
    • (1994) Acta Cryst. D , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, WA (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 25
    • 85030280545 scopus 로고    scopus 로고
    • Program and examples on maximum likelihood refinement
    • (Bailey, S., Dodson, E. & Moore, M., eds), SERC Daresbury Laboratory, Warrington, UK
    • Murshudov, G., Dodson, E. & Vagin, A. (1996). Program and examples on maximum likelihood refinement. In Proceedings of the CCP4 Study Weekend (Bailey, S., Dodson, E. & Moore, M., eds), SERC Daresbury Laboratory, Warrington, UK.
    • (1996) Proceedings of the CCP4 Study Weekend
    • Murshudov, G.1    Dodson, E.2    Vagin, A.3
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, No 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The protein data bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.