메뉴 건너뛰기




Volumn 15, Issue 19, 1996, Pages 5125-5134

Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis

Author keywords

Amidotransferases; ATP pyrophophatases; Bacillus subtilis; Enzyme structure; NAD+ synthetase

Indexed keywords

INORGANIC PYROPHOSPHATASE; MAGNESIUM ION; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYROPHOSPHATE; SYNTHETASE; AMIDE SYNTHASE; AMMONIA; LIGASE; NAD+ SYNTHASE; RECOMBINANT PROTEIN;

EID: 0029789527     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00896.x     Document Type: Article
Times cited : (80)

References (40)
  • 1
    • 0016761674 scopus 로고
    • Mutant of Bacillus subtlis with a temperature-sensitive lesion in ribonucleic acid synthesis during germination
    • Albertini, A.M. and Galizzi, A. (1975) Mutant of Bacillus subtlis with a temperature-sensitive lesion in ribonucleic acid synthesis during germination. J. Bacteriol., 124, 14-25.
    • (1975) J. Bacteriol. , vol.124 , pp. 14-25
    • Albertini, A.M.1    Galizzi, A.2
  • 3
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992b) The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 5
    • 37049090798 scopus 로고
    • Comparison of the coordinative behaviour of calcium (II) and magnesium (II) from crystallographic data
    • Carugo, O., Djinovic, K. and Rizzi, M. (1993) Comparison of the coordinative behaviour of calcium (II) and magnesium (II) from crystallographic data. J. Chem. Soc. Dalton Trans., 2127-2135.
    • (1993) J. Chem. Soc. Dalton Trans. , pp. 2127-2135
    • Carugo, O.1    Djinovic, K.2    Rizzi, M.3
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-767.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-767
  • 7
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N.P. and Brick, P. (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4, 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 9
    • 79952608525 scopus 로고
    • Accurate bond angles and parameters for X-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond angles and parameters for X-ray protein structure refinement. Acta Crystallogr., A45, 392-400.
    • (1991) Acta Crystallogr. , vol.A45 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 10
    • 0023657031 scopus 로고
    • Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
    • Fersth, A.R. (1987) Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis. Biochemistry, 26, 8031-8037.
    • (1987) Biochemistry , vol.26 , pp. 8031-8037
    • Fersth, A.R.1
  • 11
    • 0018851537 scopus 로고
    • Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems
    • Foster, J.W. and Moat, A.G. (1980) Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev., 44, 83-105.
    • (1980) Microbiol. Rev. , vol.44 , pp. 83-105
    • Foster, J.W.1    Moat, A.G.2
  • 12
    • 0017082749 scopus 로고
    • A recombination test to classify mutants of Bacillus subtilis of identical phenotype
    • Galizzi, A., Siccardi, A.G., Mazza, G., Canosi, U. and Polsinelli, M. (1976) A recombination test to classify mutants of Bacillus subtilis of identical phenotype. Genet. Res., 27, 47-58.
    • (1976) Genet. Res. , vol.27 , pp. 47-58
    • Galizzi, A.1    Siccardi, A.G.2    Mazza, G.3    Canosi, U.4    Polsinelli, M.5
  • 13
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol, W.G.J., van Duijnen, P.T. and Berendsen, H.J.C. (1978) The α-helix dipole and the properties of proteins. Nature, 273, 443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 14
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 15
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S. and Chothia, C. (1988) Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol., 204, 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 16
    • 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. and Kjeldgaard, M. (1991) Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 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. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 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
  • 20
    • 0014202619 scopus 로고
    • Molecular uniformity in biological catalyses. The enzymes concerned with firefly luciferin, amino acid, and fatty acid utilization are compared
    • McElroy, W.D., DeLuca, M. and Travis, J. (1967) Molecular uniformity in biological catalyses. The enzymes concerned with firefly luciferin, amino acid, and fatty acid utilization are compared. Science, 157, 150-160.
    • (1967) Science , vol.157 , pp. 150-160
    • McElroy, W.D.1    DeLuca, M.2    Travis, J.3
  • 21
    • 84920325457 scopus 로고
    • AMoRe: An automated procedure for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated procedure for molecular replacement. Acta Crystallogr., A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0028934050 scopus 로고
    • The outB gene of Bacillus subtlis codes for NAD synthetase
    • Nessi, C., Albertini, A.M., Speranza, M.L. and Galizzi, A. (1995) The outB gene of Bacillus subtlis codes for NAD synthetase. J. Biol. Chem., 270, 6181-6185.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6181-6185
    • Nessi, C.1    Albertini, A.M.2    Speranza, M.L.3    Galizzi, A.4
  • 23
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • Wolf, W., Evans, P.R. and Leslie, A.G.W. (eds), Isomorphous Replacement and Anomalous Scattering. SERC, Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991) Maximum likelihood refinement of heavy atom parameters. In Wolf, W., Evans, P.R. and Leslie, A.G.W. (eds), Isomorphous Replacement and Anomalous Scattering. Proceedings of the CCP4 Study Weekend 25-26 January 1991. SERC, Daresbury Laboratory, Warrington, UK, pp. 80-86.
    • (1991) Proceedings of the CCP4 Study Weekend 25-26 January 1991 , pp. 80-86
    • Otwinowski, Z.1
  • 24
    • 0027165755 scopus 로고
    • Structural basis for transfer RNA aminoacylation by Escherichia coli glutamyl-tRNA synthetase
    • Perona, J.J., Rould, M. and Steitz, T.A. (1993) Structural basis for transfer RNA aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Biochemistry, 32, 8758-8771.
    • (1993) Biochemistry , vol.32 , pp. 8758-8771
    • Perona, J.J.1    Rould, M.2    Steitz, T.A.3
  • 25
    • 0013484996 scopus 로고
    • Density modification: Theory and practice
    • Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Oxford University Press, Oxford
    • Podjarny, A.D. and Rees, B. (1991) Density modification: theory and practice. In Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Crystallographic Computing 5: From Chemistry to Biology. Oxford University Press, Oxford, pp. 361-372.
    • (1991) Crystallographic Computing 5: From Chemistry to Biology , pp. 361-372
    • Podjarny, A.D.1    Rees, B.2
  • 27
    • 0002660809 scopus 로고
    • The detections of sub-units within the crystallographic asymmetric unit
    • Rossmann, M.G. and Blow, D.M. (1962) The detections of sub-units within the crystallographic asymmetric unit. Acta Crystallogr., 15, 24-31.
    • (1962) Acta Crystallogr. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 29
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz, G.E. (1992) Binding of nucleotides by proteins. Curr. Opin. Struct. Biol., 2, 61-67.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 30
    • 0002918520 scopus 로고
    • Heavy atom location using SHELXS-90
    • Isomorphous Replacement and Anomalous Scattering. SERC, Daresbury Laboratory, Warrington, UK
    • Sheldrick, G.M. (1991) Heavy atom location using SHELXS-90. In Isomorphous Replacement and Anomalous Scattering. Proceedings of the CCP4 Study Weekend 25-26 January 1991. SERC, Daresbury Laboratory, Warrington, UK, pp. 23-38.
    • (1991) Proceedings of the CCP4 Study Weekend 25-26 January 1991 , pp. 23-38
    • Sheldrick, G.M.1
  • 31
    • 0029560755 scopus 로고
    • Enzymes of nucleotide synthesis
    • Smith, L.J. (1995) Enzymes of nucleotide synthesis. Curr. Opin. Struct. Biol., 5, 752-757.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 752-757
    • Smith, L.J.1
  • 32
    • 0014197672 scopus 로고
    • Biosynthesis of diphosphopyridine nucleotide: The purification and the properties of diphosphopyridine nucleotide synthetase from Escherichia coli
    • Spencer, R.L. and Preiss, J. (1967) Biosynthesis of diphosphopyridine nucleotide: the purification and the properties of diphosphopyridine nucleotide synthetase from Escherichia coli. J. Biol. Chem., 242, 385-392.
    • (1967) J. Biol. Chem. , vol.242 , pp. 385-392
    • Spencer, R.L.1    Preiss, J.2
  • 33
    • 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.G., Klem, T.J., Deras, M.L., Davisson, V.J. and Smith, J. (1996) The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nature Struct. Biol., 3, 74-86.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 74-86
    • Tesmer, J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.5
  • 34
    • 0000888502 scopus 로고
    • The locked rotation function
    • Tong, L. and Rossmann, M.G. (1990) The locked rotation function. Acta Crystallogr., A46, 783-792.
    • (1990) Acta Crystallogr. , vol.A46 , pp. 783-792
    • Tong, L.1    Rossmann, M.G.2
  • 35
    • 0001005516 scopus 로고
    • NAD biosynthesis and recycling
    • Neidhardt, F.C., Ingraham, J.L., Brooks Low, K., Magasanik, B., Schaechter, M. and Umbarger, H.E. (eds), American Society for Microbiology, Washington DC
    • Tritz, G.J. (1987) NAD biosynthesis and recycling. In Neidhardt, F.C., Ingraham, J.L., Brooks Low, K., Magasanik, B., Schaechter, M. and Umbarger, H.E. (eds), Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology. American Society for Microbiology, Washington DC, Vol. 1, pp. 557-563.
    • (1987) Escherichia Coli and Salmonella Typhimurium Cellular and Molecular Biology , vol.1 , pp. 557-563
    • Tritz, G.J.1
  • 36
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. and Matthews, B.W. (1987) An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr., A43, 489-501.
    • (1987) Acta Crystallogr. , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 37
    • 0001280470 scopus 로고
    • DEMON/ANGEL: A suite of programs to carry out density modification
    • Vellieux, F.M.D.V., Hunt, J.F., Roy, S. and Read, R.J. (1995) DEMON/ANGEL: a suite of programs to carry out density modification. J. Appl. Crystallogr., 28, 347-351.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 347-351
    • Vellieux, F.M.D.V.1    Hunt, J.F.2    Roy, S.3    Read, R.J.4
  • 38
    • 0002023468 scopus 로고
    • Biosynthesis of salvage pathaways of pyridine nucleotide coenzymes
    • Everse, J., Anderson, B.M. and You, K.S. (eds), Academic Press Inc., New York
    • White, H.B. (1982) Biosynthesis of salvage pathaways of pyridine nucleotide coenzymes. In Everse, J., Anderson, B.M. and You, K.S. (eds), Pyridine Nucleotide Coenzyme. Academic Press Inc., New York, pp. 1-17.
    • (1982) Pyridine Nucleotide Coenzyme , pp. 1-17
    • White, H.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.