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Volumn 89, Issue 4, 1997, Pages 545-553

X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

EID: 0038228666     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80236-6     Document Type: Article
Times cited : (221)

References (29)
  • 1
    • 0028833053 scopus 로고
    • Reaction in alphavirus mRNA capping: Formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP
    • Ahola, T., and Kaariainen, L. (1995). Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP. Proc. Natl. Acad. Sci. USA 92, 507-511.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 507-511
    • Ahola, T.1    Kaariainen, L.2
  • 2
    • 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, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 3
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A.T., Karplus, M., and Petsko, G.A. (1989).Crystallographic refinement by simulated annealing: application to crambin. Acta Cryst. A45, 50-61.
    • (1989) Acta Cryst. , vol.A45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 4
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. (1991). Ribbons 2.0. J. Appl. Cryst. 24, 958-961.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 958-961
    • Carson, M.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 6
    • 0027408354 scopus 로고
    • Covalent catalysis in nucleotidyl transfer. A KTDG motif essential for enzyme - GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases
    • Cong, P., and Shuman, S. (1993). Covalent catalysis in nucleotidyl transfer. A KTDG motif essential for enzyme - GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases. J. Biol. Chem. 268, 7256-7260.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7256-7260
    • Cong, P.1    Shuman, S.2
  • 7
    • 0028862970 scopus 로고
    • Mutational analysis of messenger-RNA capping enzyme identifies amino acids involved in GTP-binding, enzyme-guanylate formation and GMP transfer to DNA
    • Cong, P., and Shuman, S. (1995). Mutational analysis of messenger-RNA capping enzyme identifies amino acids involved in GTP-binding, enzyme-guanylate formation and GMP transfer to DNA. Mol. Cell. Biol. 15, 6222-6231.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6222-6231
    • Cong, P.1    Shuman, S.2
  • 8
    • 0029906410 scopus 로고    scopus 로고
    • Characterisation of proteolytic fragments of bacteriophage T7 DNA ligase
    • Doherty, A.J., Ashford, S.R., Subramanya, H.S., and Wigley, D.B. (1996). Characterisation of proteolytic fragments of bacteriophage T7 DNA ligase. Nucl. Acids Res. 24, 2281-2287.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2281-2287
    • Doherty, A.J.1    Ashford, S.R.2    Subramanya, H.S.3    Wigley, D.B.4
  • 10
    • 0028214041 scopus 로고
    • Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: Similarity to the nucleotidyl attachment motif of DNA and RNA ligases
    • Fresco, L.D. and Buratowski, S. (1994). Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases. Proc. Natl. Acad. Sci. USA 91, 6624-6628.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6624-6628
    • Fresco, L.D.1    Buratowski, S.2
  • 11
    • 0023663357 scopus 로고
    • Effect of single amino acid changes in the region of the adenylation site of T4 RNA ligase
    • Heaphy, S., Singh, M., and Gait, M.J. (1987). Effect of single amino acid changes in the region of the adenylation site of T4 RNA ligase. Biochemistry 26, 1688-1696.
    • (1987) Biochemistry , vol.26 , pp. 1688-1696
    • Heaphy, S.1    Singh, M.2    Gait, M.J.3
  • 12
    • 0029817880 scopus 로고    scopus 로고
    • Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1
    • Ho, C.K., van Etten, J.L. and Shuman, S. (1996). Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1. J. Virol. 70, 6658-6664.
    • (1996) J. Virol. , vol.70 , pp. 6658-6664
    • Ho, C.K.1    Van Etten, J.L.2    Shuman, S.3
  • 13
    • 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., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
    • (1991) Acta Cryst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.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. and 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
    • 0001173909 scopus 로고
    • Transition state stabilisation in the mechanism of tyrosyl transfer RNA synthetase revealed by protein engineering
    • Leatherbarrow, R.J., Fersht, A.R., and Winter, G. (1985). Transition state stabilisation in the mechanism of tyrosyl transfer RNA synthetase revealed by protein engineering. Proc. Natl. Acad. Sci. USA 82, 7840-7844.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7840-7844
    • Leatherbarrow, R.J.1    Fersht, A.R.2    Winter, G.3
  • 16
    • 0028803831 scopus 로고
    • Analysis of 43KB of the Chlorella virus PBCV-1 330KB genome - Map positions 45-88
    • Li, Y., Lu, Z.Q., Burbank, P.E., Kutish, G.F., Rock, D.L., and Vanetten, J.L. (1995). Analysis of 43KB of the Chlorella virus PBCV-1 330KB genome - Map positions 45-88. Virology 212, 134-150.
    • (1995) Virology , vol.212 , pp. 134-150
    • Li, Y.1    Lu, Z.Q.2    Burbank, P.E.3    Kutish, G.F.4    Rock, D.L.5    Vanetten, J.L.6
  • 17
    • 84986486656 scopus 로고
    • A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the poisson-Boltzmann equation
    • Nicholls, A., and Honig, B.J. (1991). A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem. 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.J.2
  • 18
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • S.E.R.C. Daresbury DL/SC1/R34
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, S.E.R.C. Daresbury DL/SC1/R34, pp. 56-62.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 19
    • 0028211258 scopus 로고
    • Mutational analysis of yeast mRNA capping enzyme
    • Schwer, B., and Shuman, S. (1994) Mutational analysis of yeast mRNA capping enzyme. Proc. Natl. Acad. Sci. USA 91, 4328-4332.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4328-4332
    • Schwer, B.1    Shuman, S.2
  • 20
    • 0000728003 scopus 로고
    • D. Moras, A.D. Podjarny, and J.G. Thierry, eds. (Oxford, U.K.: Oxford University Press)
    • Sheldrick, G. (1992). In Crystallographic Computing 5, D. Moras, A.D. Podjarny, and J.G. Thierry, eds. (Oxford, U.K.: Oxford University Press), pp. 145-157.
    • (1992) Crystallographic Computing , vol.5 , pp. 145-157
    • Sheldrick, G.1
  • 21
    • 0026733001 scopus 로고
    • MRNA capping enzyme: Isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae
    • Shibagaki, Y., Itoh, N., Yamada, H., Nagata, S., and Mizumoto, K. (1992). mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae. J. Biol. Chem. 267, 9521-9528.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9521-9528
    • Shibagaki, Y.1    Itoh, N.2    Yamada, H.3    Nagata, S.4    Mizumoto, K.5
  • 22
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman, S. (1995). Capping enzyme in eukaryotic mRNA synthesis. Prog. Nucl. Acids Res. Mol. Biol. 50, 101-129.
    • (1995) Prog. Nucl. Acids Res. Mol. Biol. , vol.50 , pp. 101-129
    • Shuman, S.1
  • 23
    • 0030585422 scopus 로고    scopus 로고
    • Closing the gap on DNA ligase
    • Shuman, S. (1996). Closing the gap on DNA ligase. Structure 4, 653-656.
    • (1996) Structure , vol.4 , pp. 653-656
    • Shuman, S.1
  • 24
    • 0000262312 scopus 로고
    • Mechanism of mRNAcapping by vaccinia virus guanylyltransferase: Characterization of an enzyme-guanylate intermediate
    • Shuman S., and Hurwitz, J. (1981). Mechanism of mRNAcapping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate. Proc. Natl. Acad. Sci. USA 78, 187-191.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 187-191
    • Shuman, S.1    Hurwitz, J.2
  • 25
    • 0028172876 scopus 로고
    • Covalent catalysis in nucleotidyl transfer reactions: Essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases
    • Shuman, S., Liu, Y., and Schwer, B. (1994). Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases. Proc. Natl. Acad. Sci. USA 91, 12046-12050.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12046-12050
    • Shuman, S.1    Liu, Y.2    Schwer, B.3
  • 26
    • 0029152217 scopus 로고
    • Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis
    • Shuman, S., and Ru, X.-M. (1995). Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis. Virology 211, 73-83.
    • (1995) Virology , vol.211 , pp. 73-83
    • Shuman, S.1    Ru, X.-M.2
  • 27
    • 0029056990 scopus 로고
    • RNA capping enzyme and DNA ligase: A superfamily of covalent nucleotide transferases
    • Shuman, S., and Schwer, B. (1995). RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotide transferases. Mol. Microbiol. 17, 405-410.
    • (1995) Mol. Microbiol. , vol.17 , pp. 405-410
    • Shuman, S.1    Schwer, B.2
  • 28
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R., and Wigley, D.B. (1996). Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell 85, 607-614.
    • (1996) Cell , vol.85 , pp. 607-614
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 29
    • 0029764473 scopus 로고    scopus 로고
    • Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from candida albicans
    • Yamada-Okabe, T., Shimmi, O., Doi, R., Mizumoto, K., Arisawa, M., and Yamada-Okabe, H. (1996). Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans. Microbiology 141, 2515-2523.
    • (1996) Microbiology , vol.141 , pp. 2515-2523
    • Yamada-Okabe, T.1    Shimmi, O.2    Doi, R.3    Mizumoto, K.4    Arisawa, M.5    Yamada-Okabe, H.6


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