메뉴 건너뛰기




Volumn 438, Issue 7067, 2005, Pages 520-524

An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; ESTERS; HYDROLYSIS; SUBSTRATES;

EID: 28544452248     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04152     Document Type: Article
Times cited : (305)

References (29)
  • 1
    • 0037145032 scopus 로고    scopus 로고
    • The path to perdition is paved with protons
    • Green, R. & Lorsch, J. R. The path to perdition is paved with protons. Cell 110, 665-668 (2002).
    • (2002) Cell , vol.110 , pp. 665-668
    • Green, R.1    Lorsch, J.R.2
  • 3
    • 0000589080 scopus 로고
    • eds Boyer, P. D., Lardy, H. & Myrback, K. Academic, New York
    • Koshland, D. E. in The Enzymes (eds Boyer, P. D., Lardy, H. & Myrback, K.) 305-346 (Academic, New York, 1959).
    • (1959) The Enzymes , pp. 305-346
    • Koshland, D.E.1
  • 4
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennett, W. S. Jr & Steitz, T. A. Glucose-induced conformational change in yeast hexokinase. Proc. Natl Acad. Sci. USA 75, 4848-4852 (1978).
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4848-4852
    • Bennett Jr., W.S.1    Steitz, T.A.2
  • 6
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov, A. V., Mora, L., Buckingham, R. H. & Ehrenberg, M. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell 10, 789-798 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 7
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed, D. & Noller, H. F. Intermediate states in the movement of transfer RNA in the ribosome. Nature 342, 142-148 (1989).
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 8
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape, T., Wintermeyer, W. & Rodnina, M. Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18, 3800-3807 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 9
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • Katunin, V. I., Muth, G. W., Strobel, S. A., Wintermeyer, W. & Rodnina, M. V. Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome. Mol. Cell 10, 339-346 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 339-346
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 10
    • 0036177483 scopus 로고    scopus 로고
    • A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits
    • Schmeing, T. M. et al. A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nature Struct. Biol. 9, 225-230 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 225-230
    • Schmeing, T.M.1
  • 11
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P. B. & Steitz, T. A. The structural basis of ribosome activity in peptide bond synthesis. Science 289, 920-930 (2000).
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 12
    • 2542445275 scopus 로고    scopus 로고
    • Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
    • Agmon, I. et al. Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. FEBS Lett. 567, 20-26 (2004).
    • (2004) FEBS Lett. , vol.567 , pp. 20-26
    • Agmon, I.1
  • 14
    • 33947086888 scopus 로고
    • Geometrical reaction coordinates. II. Nucleophilic addition to a carbonyl group
    • Burgi, H. B., Dunitz, J. D. & Shefter, E. Geometrical reaction coordinates. II. Nucleophilic addition to a carbonyl group. J. Am. Chem. Soc. 95, 5065-5067 (1973).
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 5065-5067
    • Burgi, H.B.1    Dunitz, J.D.2    Shefter, E.3
  • 15
    • 0036678453 scopus 로고    scopus 로고
    • A clogged gutter mechanism for protease inhibitors
    • Radisky, E. S. & Koshland, D. E. Jr. A clogged gutter mechanism for protease inhibitors. Proc. Natl Acad. Sci. USA 99, 10316-10321 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10316-10321
    • Radisky, E.S.1    Koshland Jr., D.E.2
  • 16
    • 2942615089 scopus 로고    scopus 로고
    • The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit
    • Klein, D. J., Moore, P. B. & Steitz, T. A. The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J. Mol. Biol. 340, 141-177 (2004).
    • (2004) J. Mol. Biol. , vol.340 , pp. 141-177
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 19
    • 0142178293 scopus 로고    scopus 로고
    • Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit
    • Schmeing, T. M., Moore, P. B. & Steitz, T. A. Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA 9, 1345-1352 (2003).
    • (2003) RNA , vol.9 , pp. 1345-1352
    • Schmeing, T.M.1    Moore, P.B.2    Steitz, T.A.3
  • 20
    • 14844352639 scopus 로고    scopus 로고
    • Kinetic isotope effect analysis of the ribosomal peptidyl transferase reaction
    • Seila, A. C., Okuda, K., Nunez, S., Seila, A. F. & Strobel, S. A. Kinetic isotope effect analysis of the ribosomal peptidyl transferase reaction. Biochemistry 44, 4018-4027 (2005).
    • (2005) Biochemistry , vol.44 , pp. 4018-4027
    • Seila, A.C.1    Okuda, K.2    Nunez, S.3    Seila, A.F.4    Strobel, S.A.5
  • 21
    • 0038012848 scopus 로고    scopus 로고
    • Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2
    • Scarlett, D. J., McCaughan, K. K., Wilson, D. N. & Tate, W. P. Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2. J. Biol. Chem. 278, 15095-15104 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 15095-15104
    • Scarlett, D.J.1    McCaughan, K.K.2    Wilson, D.N.3    Tate, W.P.4
  • 22
    • 0347721768 scopus 로고    scopus 로고
    • A cryo-electron microscopic study of ribosome-bound termination factor RF2
    • Rawat, U. B. et al. A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421, 87-90 (2003).
    • (2003) Nature , vol.421 , pp. 87-90
    • Rawat, U.B.1
  • 23
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • Frolova, L. Y. et al. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5, 1014-1020 (1999).
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1
  • 24
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E. M., Brunelle, J. L., Kochaniak, A. B. & Green, R. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell 117, 589-599 (2004).
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 25
    • 2542526957 scopus 로고    scopus 로고
    • Solid phase synthesis and binding affinity of peptidyl transferase transition state mimics containing 2′-OH at P-site position A76
    • Weinger, J. S., Kitchen, D., Scaringe, S. A., Strobel, S. A. & Muth, G. W. Solid phase synthesis and binding affinity of peptidyl transferase transition state mimics containing 2′-OH at P-site position A76. Nucleic Acids Res. 32, 1502-1511 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1502-1511
    • Weinger, J.S.1    Kitchen, D.2    Scaringe, S.A.3    Strobel, S.A.4    Muth, G.W.5
  • 26
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B. & Steitz, T. A. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289, 905-920 (2000).
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 29
    • 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.