메뉴 건너뛰기




Volumn 5, Issue 7, 1997, Pages 895-906

Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: A new family of adenine nucleotide α hydrolase

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0031571084     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00244-X     Document Type: Article
Times cited : (53)

References (46)
  • 1
    • 0039399893 scopus 로고
    • Biochemistry of the sulfur cycle
    • (D.M. Greenberg, ed.), Academic Press, New York
    • Siegel, L.M. (1975). Biochemistry of the sulfur cycle. In Metabolism of Sulfur Compounds. Metabolic pathways (D.M. Greenberg, ed.), pp. 217-286, Academic Press, New York.
    • (1975) Metabolism of Sulfur Compounds. Metabolic Pathways , pp. 217-286
    • Siegel, L.M.1
  • 3
    • 12644307044 scopus 로고    scopus 로고
    • Assimilatory reduction of inorganic sulphate
    • (J.W. Cram, ed.), Academic Publishing, The Hague
    • Schwenn, J.D. (1997). Assimilatory reduction of inorganic sulphate. In Sulfur nutrition and assimilation in higher plants (J.W. Cram, ed.), pp. 3-23, Academic Publishing, The Hague.
    • (1997) Sulfur Nutrition and Assimilation in Higher Plants , pp. 3-23
    • Schwenn, J.D.1
  • 4
    • 0014939566 scopus 로고
    • The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate
    • Porque, P.G., Baldestein, A. & Reichard, P. (1970). The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate. J. Biol. Chem. 245, 2371-2374.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2371-2374
    • Porque, P.G.1    Baldestein, A.2    Reichard, P.3
  • 5
    • 0010595016 scopus 로고
    • Function of thioredoxin in the reduction of adenosine 3•-phosphate 5•-phosphosulfate in Escherichia coli
    • (Gadal, P., ed.), Edt. du CNRS, Paris
    • Tsang, M.L.-S. (1983). Function of thioredoxin in the reduction of adenosine 3•-phosphate 5•-phosphosulfate in Escherichia coli. In Thioredoxins: Structure and Functions (Gadal, P., ed.), pp. 21-24, Edt. du CNRS, Paris.
    • (1983) Thioredoxins: Structure and Functions , pp. 21-24
    • Tsang, M.L.-S.1
  • 6
    • 0028849610 scopus 로고
    • Reaction mechanism of thioredoxin: 3-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis
    • Behrendt, U., Haverkamp, T., Prior, A. & Schwenn, J.D. (1995). Reaction mechanism of thioredoxin: 3-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233, 347-356.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 347-356
    • Behrendt, U.1    Haverkamp, T.2    Prior, A.3    Schwenn, J.D.4
  • 7
    • 0028809514 scopus 로고
    • Sulphite reductase structure at 1.6 Å resolution: Evolution and catalysis for reduction of inorganic anions
    • Crane, B.R., Siegel, L.M. & Getzoff, E.D. (1995). Sulphite reductase structure at 1.6 Å resolution: evolution and catalysis for reduction of inorganic anions. Science 270, 59-67.
    • (1995) Science , vol.270 , pp. 59-67
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3
  • 9
    • 0025924684 scopus 로고
    • Characterization of the gene cysH and of its product phospho-adenylylsulphate reductase from E. coli
    • Krone, F.A, Westphal, G. & Schwenn, J.D. (1991). Characterization of the gene cysH and of its product phospho-adenylylsulphate reductase from E. coli. Mol. Gen. Genet. 225, 315-319.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 315-319
    • Krone, F.A.1    Westphal, G.2    Schwenn, J.D.3
  • 10
    • 0024298590 scopus 로고
    • Directed mutagenesis indicates that the donor to P+680 in photosystem II is tyrosine-161 of the D1 polypeptide
    • Debus, R.J., Barry, B.A., Sithole, I., Babcock, G.T. & McIntosh, L. (1988). Directed mutagenesis indicates that the donor to P+680 in photosystem II is tyrosine-161 of the D1 polypeptide. Biochemistry 27, 9071-9074.
    • (1988) Biochemistry , vol.27 , pp. 9071-9074
    • Debus, R.J.1    Barry, B.A.2    Sithole, I.3    Babcock, G.T.4    McIntosh, L.5
  • 11
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B.-M. & Eklund, H. (1990). Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-398.
    • (1990) Nature , vol.345 , pp. 593-1398
    • Nordlund, P.1    Sjöberg, B.-M.2    Eklund, H.3
  • 12
    • 0023024626 scopus 로고
    • The glycine-rich loop of adenylate kinase forms a giant anion hole
    • Dreusicke, D. & Schulz, G.E. (1986). The glycine-rich loop of adenylate kinase forms a giant anion hole. FEBS Lett. 208, 301-304.
    • (1986) FEBS Lett. , vol.208 , pp. 301-304
    • Dreusicke, D.1    Schulz, G.E.2
  • 13
    • 0025048136 scopus 로고
    • The 'P-loop' - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R. & Wittinghofer, A. (1990). The 'P-loop' - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 14
    • 0028559230 scopus 로고
    • A P-loop-like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity
    • Bork, P. & Koonin, E.V. (1994). A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. Proteins 20, 347-355.
    • (1994) Proteins , vol.20 , pp. 347-355
    • Bork, P.1    Koonin, E.V.2
  • 15
    • 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, J.L. (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.L.5
  • 16
    • 0029645124 scopus 로고
    • Structural analysis of human • -class glutathione transferase A1-1 in the apo-form and in complex with ethycrynic acid and its glutathione conjugate
    • Cameron, A.D., et al., & Jones, T.A. (1995). Structural analysis of human • -class glutathione transferase A1-1 in the apo-form and in complex with ethycrynic acid and its glutathione conjugate. Structure 3, 717-727.
    • (1995) Structure , vol.3 , pp. 717-727
    • Cameron, A.D.1    Jones, T.A.2
  • 17
    • 0025398721 scopus 로고
    • WHATIF: A molecular modeling and drug design program
    • Vriend, G. (1990). WHATIF: a molecular modeling and drug design program. J. Mol. Graphics 8, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 19
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & 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
  • 20
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T.A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Cryst. 11, 268-272.
    • (1978) J. Appl. Cryst. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 21
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, TA., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for the building of protein 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
  • 22
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz, G. (1993). Binding of nucleotides by proteins. Curr. Opin. Struct. Biol. 2, 61-67.
    • (1993) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.1
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 282.
    • (1991) Proteins , vol.11 , pp. 282
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 24
    • 0027501461 scopus 로고
    • Anion-binding sites in protein structures
    • Chakrabarti, P. (1993). Anion-binding sites in protein structures. J. Mol. Biol. 234, 463-482.
    • (1993) J. Mol. Biol. , vol.234 , pp. 463-482
    • Chakrabarti, P.1
  • 25
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phospho-glycerate kinase and its substrate 3-phospho-D-glycerate
    • Harlos, K., Vas, M. & Blake, C.F. (1992). Crystal structure of the binary complex of pig muscle phospho-glycerate kinase and its substrate 3-phospho-D-glycerate. Proteins 13, 133-144.
    • (1992) Proteins , vol.13 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 27
    • 0024406896 scopus 로고
    • Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate
    • Brick, P., Bhat, T.N. & Blow, D.M. (1989). Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. J. Mol. Biol. 208, 83-98.
    • (1989) J. Mol. Biol. , vol.208 , pp. 83-98
    • Brick, P.1    Bhat, T.N.2    Blow, D.M.3
  • 28
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould, M.A., Perona, J.J. & Steitz, T.A. (1991). Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352, 213-218.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 29
    • 0001281761 scopus 로고
    • Protein tyrosine sulfation
    • Huttner, W. (1987). Protein tyrosine sulfation. Trends Biochem. Sci. 12, 361-363.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 361-363
    • Huttner, W.1
  • 30
    • 0025340754 scopus 로고
    • Induced-fit movements in adenylate kinases
    • Schulz, G.E., Müller, C.W. & Diederichs, K. (1990). Induced-fit movements in adenylate kinases. J. Mol. Biol. 213, 627-630.
    • (1990) J. Mol. Biol. , vol.213 , pp. 627-630
    • Schulz, G.E.1    Müller, C.W.2    Diederichs, K.3
  • 31
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers
    • Gerstein, M., Schulz, G. & Chothia,C. (1993). Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers. J. Mol. Biol. 229, 494-501.
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.2    Chothia, C.3
  • 32
    • 0032032244 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction study of phosphoadenylylsulfate (PAPS) reductase from E. coli
    • in press
    • Montoya, G., Svensson, C., Savage, H., Schwenn, J.D. & Sinning, I. (1997). Crystallization and preliminary X-ray diffraction study of phosphoadenylylsulfate (PAPS) reductase from E. coli. Acta Cryst. D, in press.
    • (1997) Acta Cryst. D
    • Montoya, G.1    Svensson, C.2    Savage, H.3    Schwenn, J.D.4    Sinning, I.5
  • 33
    • 0014432781 scopus 로고
    • Solvent content in proteins
    • Matthews, B.W. (1968). Solvent content in proteins. J. Mol. Biol. 33, 491.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491
    • Matthews, B.W.1
  • 34
    • 0002452464 scopus 로고
    • Oscillation Data Reduction Program
    • (Sawyer, NI & Bailey, S., Eds), Science and Engineering Research Council Daresbury Laboratory, Daresbury, UK
    • Otwinowski, Z. (1993). Oscillation Data Reduction Program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Sawyer, NI & Bailey, S., Eds), pp. 56-62, Science and Engineering Research Council Daresbury Laboratory, Daresbury, UK.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 35
    • 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 Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 36
    • 0002701928 scopus 로고
    • PHASES:a program package for the processing and analysis of diffraction data from macromolecules
    • Series 2
    • Furey, W. & Swaminathan, S. (1990). PHASES:a program package for the processing and analysis of diffraction data from macromolecules. In American Crystallographic Association Meeting Abstracts. Series 2, Vol. 18, pp73.
    • (1990) American Crystallographic Association Meeting Abstracts , vol.18 , pp. 73
    • Furey, W.1    Swaminathan, S.2
  • 38
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-473.
    • (1992) Nature , vol.355 , pp. 472-473
    • Brünger, A.T.1
  • 39
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 40
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, S.D. & Thornton, J.M.J. (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, S.D.3    Thornton, J.M.J.4
  • 41
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide chain conformations. Allowed conformations for a pair of peptide units
    • Ramakrishnan, C. & Ramachandran, G.N. (1965). Stereochemical criteria for polypeptide chain conformations. Allowed conformations for a pair of peptide units. Biophys. J. 5, 909-933.
    • (1965) Biophys. J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 43
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 44
    • 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
  • 45
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 46
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments, Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.