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Volumn 262, Issue 4, 1996, Pages 502-515

The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: Effects of ionic strength

Author keywords

Crystal packing; Hyperthermophiles; Indole 3 glycerol phosphate synthase; Ionic strength; Salt bridges

Indexed keywords

AMMONIUM SULFATE; ANION; ETHYLENE GLYCOL; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE; MACROGOL DERIVATIVE; OXYGEN;

EID: 0030568997     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0531     Document Type: Article
Times cited : (31)

References (41)
  • 1
    • 0028088670 scopus 로고
    • Indole-3-glycerol-phosphate synthase from Sulfolobus solfataricus as a model for studying thermostable TIM-barrel enzymes
    • Andreotti, G., Tutino, M. L., Sannia, G., Marino, G. & Cubellis, M. V. (1994). Indole-3-glycerol-phosphate synthase from Sulfolobus solfataricus as a model for studying thermostable TIM-barrel enzymes. Biochim. Biophys. Acta, 1208, 310-315.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 310-315
    • Andreotti, G.1    Tutino, M.L.2    Sannia, G.3    Marino, G.4    Cubellis, M.V.5
  • 5
    • 0018644845 scopus 로고
    • N-(5′-phosphoribosyl) anthranilate isomerase - Indoleglycerol-phosphate synthase 1. A substrate analogue binds to two different binding sites on the bifunctional enzyme from Escherichia coli
    • Bisswanger, H., Kirschner, K., Cohn, W., Hager, V. & Hansson, E. (1979). N-(5′-phosphoribosyl) anthranilate isomerase - indoleglycerol-phosphate synthase 1. A substrate analogue binds to two different binding sites on the bifunctional enzyme from Escherichia coli. Biochemistry, 18, 5946-5953.
    • (1979) Biochemistry , vol.18 , pp. 5946-5953
    • Bisswanger, H.1    Kirschner, K.2    Cohn, W.3    Hager, V.4    Hansson, E.5
  • 7
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4: Programs for protein crystallography
    • CCP4 (1994). Collaborative Computational Project, Number 4: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 8
    • 0014028006 scopus 로고
    • Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon
    • Creighton, T. E. & Yanofsky, C. (1966). Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J. Biol. Chem. 241, 4616-4624.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4616-4624
    • Creighton, T.E.1    Yanofsky, C.2
  • 9
    • 0030043489 scopus 로고    scopus 로고
    • Cation - π interaction in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. (1996). Cation - π interaction in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science, 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.1
  • 11
    • 0029003832 scopus 로고
    • Indoleglycerol phosphate synthase - Phosphoribosyl anthranilate isomerase: Comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains
    • Eberhard, M., Tsai-Pflugfelder, M., Bolewska, K., Hommel, U. & Kirschner, K. (1995). Indoleglycerol phosphate synthase - phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. Biochemistry, 34, 5419-5428.
    • (1995) Biochemistry , vol.34 , pp. 5419-5428
    • Eberhard, M.1    Tsai-Pflugfelder, M.2    Bolewska, K.3    Hommel, U.4    Kirschner, K.5
  • 12
    • 0029176320 scopus 로고
    • How to make my blood boil
    • Goldman, A. (1995). How to make my blood boil. Structure, 3, 1277-1279.
    • (1995) Structure , vol.3 , pp. 1277-1279
    • Goldman, A.1
  • 13
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig, M., Darimont, B., Kirschner, K. & Jansonius, J. N. (1995). 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure, 3, 1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Kirschner, K.3    Jansonius, J.N.4
  • 14
    • 0028297538 scopus 로고
    • Crystalline mitochondrial aspartate aminotransferase exists in only two conformations
    • Hohenester, E. & Jansonius, J. N. (1994). Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J. Mol. Biol. 236, 963-968.
    • (1994) J. Mol. Biol. , vol.236 , pp. 963-968
    • Hohenester, E.1    Jansonius, J.N.2
  • 15
    • 0027475153 scopus 로고
    • Helical peptides with three Asp-Arg and Glu-Arg residues in different orientations and spacings
    • Huyghues-Despointes, B. M. P., Scholtz, J. M. & Baldwin, R. L. (1993). Helical peptides with three Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Sci. 2, 80-85.
    • (1993) Protein Sci. , vol.2 , pp. 80-85
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 16
    • 0028882032 scopus 로고
    • Measuring the strength of side-chain hydrogen bonds in peptide helices: The Gin-Asp (i, i + 4) interaction
    • Huyghues-Despointes, B. M. P., Klingler, T. M. & Baldwin, R. L. (1995). Measuring the strength of side-chain hydrogen bonds in peptide helices: the Gin-Asp (i, i + 4) interaction. Biochemistry, 34, 13267-13271.
    • (1995) Biochemistry , vol.34 , pp. 13267-13271
    • Huyghues-Despointes, B.M.P.1    Klingler, T.M.2    Baldwin, R.L.3
  • 17
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of "hyperstable proteins": Glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima
    • In the press
    • Jaenicke, R., Schurig, H., Beaucamp, N. & Ostendorp, R. (1996). Structure and stability of "hyperstable proteins": glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima. Advan. Protein Chem., In the press.
    • (1996) Advan. Protein Chem.
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 18
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, T. A. (1985). Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein 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 protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21, 916-924.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 21
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. & Jaenicke, R. (1995). The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246, 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 22
    • 0026645602 scopus 로고
    • Variability of conformations at crystal contacts in BPTI represent true low-energy structures: Correspondence among lattice packing and molecular dynamics structures
    • Kossiakoff, A. A., Randal, M., Guenot, J. & Eigenbrot, C. (1992). Variability of conformations at crystal contacts in BPTI represent true low-energy structures: correspondence among lattice packing and molecular dynamics structures. Proteins: Struct. Funct. Genet. 14, 65-74.
    • (1992) Proteins: Struct. Funct. Genet. , vol.14 , pp. 65-74
    • Kossiakoff, A.A.1    Randal, M.2    Guenot, J.3    Eigenbrot, C.4
  • 23
    • 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. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 24
    • 0001513484 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. Crystallog. 26, 946-950.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 946-950
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 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
  • 27
    • 0027328752 scopus 로고
    • Structural and genetic analysis of protein folding and stability
    • Matthews, B. W. (1991). Structural and genetic analysis of protein folding and stability. Curr. Opin. Struct. Biol. 3, 589-593.
    • (1991) Curr. Opin. Struct. Biol. , vol.3 , pp. 589-593
    • Matthews, B.W.1
  • 28
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews, B. W. (1993). Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62, 139-160.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 29
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia, B., Buchner, K. & Arad, D. (1995). Complex salt bridges in proteins: statistical analysis of structure and function. J. Mol. Biol. 254, 761-770.
    • (1995) J. Mol. Biol. , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, K.2    Arad, D.3
  • 30
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaze, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A, 50, 157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaze, J.1
  • 31
    • 0027242141 scopus 로고
    • Structures of the "open" and "closed" state of tryptosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
    • Noble, M. E. M., Zeelen, J. P. & Wierenga, R. K. (1993). Structures of the "open" and "closed" state of tryptosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism. Proteins: Struct. Funct. Genet. 16, 311-326.
    • (1993) Proteins: Struct. Funct. Genet. , vol.16 , pp. 311-326
    • Noble, M.E.M.1    Zeelen, J.P.2    Wierenga, R.K.3
  • 32
    • 0023394638 scopus 로고
    • Three-dimensional structure of the bifunctional enzyme N-(5′-phosphoribosyl)anthranilate isomerase - Indole-3-glycerol phosphate synthase from Escherichia coli
    • Priestle, J. P., Grütter, M. G., White, J. L., Vincent, M. G., Kania, M., Wilson, E., Jardetzky, T. S., Kirschner, K. & Jansonius, J. N. (1987). Three-dimensional structure of the bifunctional enzyme N-(5′-phosphoribosyl)anthranilate isomerase - indole-3-glycerol phosphate synthase from Escherichia coli. Proc. Natl Acad. Sci. USA, 84, 5690-5694.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5690-5694
    • Priestle, J.P.1    Grütter, M.G.2    White, J.L.3    Vincent, M.G.4    Kania, M.5    Wilson, E.6    Jardetzky, T.S.7    Kirschner, K.8    Jansonius, J.N.9
  • 34
    • 0029645118 scopus 로고
    • The low ionic strength crystal structure of horse cytochrome c at 2.1 Å resolution and comparison with its high ionic strength counterpart
    • Sanishvili, R., Volz, K. W., Westbrook, E. M. & Margoliash, E. (1995). The low ionic strength crystal structure of horse cytochrome c at 2.1 Å resolution and comparison with its high ionic strength counterpart. Structure, 3, 707-716.
    • (1995) Structure , vol.3 , pp. 707-716
    • Sanishvili, R.1    Volz, K.W.2    Westbrook, E.M.3    Margoliash, E.4
  • 35
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz, J. M., Qian, H., Robbins, V. H. & Baldwin, R. L. (1993). The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry, 32, 9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 36
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution
    • Tanner, J. J., Hecht, R. M. & Krause, K. L. (1996). Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution. Biochemistry, 35, 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 38
    • 0026014458 scopus 로고
    • Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis
    • Wilmanns, M., Hyde, C. C., Davies, D. R., Kirschner, K. & Jansonius, J. N. (1991). Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry, 30, 9161-9169.
    • (1991) Biochemistry , vol.30 , pp. 9161-9169
    • Wilmanns, M.1    Hyde, C.C.2    Davies, D.R.3    Kirschner, K.4    Jansonius, J.N.5
  • 39
    • 0026584311 scopus 로고
    • Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: Indoleglycerol-phosphate synthase from Escherichia coli refined at 2.0 Å resolution
    • Wilmanns, M., Priestle, J. P., Niermann, Th. & Jansonius, J. N. (1992). Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerol-phosphate synthase from Escherichia coli refined at 2.0 Å resolution. J. Mol. Biol. 223, 477-507.
    • (1992) J. Mol. Biol. , vol.223 , pp. 477-507
    • Wilmanns, M.1    Priestle, J.P.2    Niermann, Th.3    Jansonius, J.N.4
  • 41
    • 0029150760 scopus 로고
    • Protein flexibility and adaptibility seen in 25 crystal forms of T4 lysozyme
    • Zhang, X.-J., Wozniak, J. A. & Matthews, B. W. (1995). Protein flexibility and adaptibility seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250, 527-552.
    • (1995) J. Mol. Biol. , vol.250 , pp. 527-552
    • Zhang, X.-J.1    Wozniak, J.A.2    Matthews, B.W.3


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