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Volumn 2, Issue 3, 1997, Pages

Macromolecular mimicry in protein biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR TU; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE;

EID: 0030628152     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00056-4     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0003110793 scopus 로고
    • Factors involved in the transfer of aminoacyl-tRNA to the ribosome
    • (Weissbach, H. & Petska, S. eds.), Academic Press, New York
    • Miller, D.L. & Weissbach, H. (1977). Factors involved in the transfer of aminoacyl-tRNA to the ribosome. In Molecular Mechanisms of Protein Biosynthesis. (Weissbach, H. & Petska, S. eds.), pp. 323-373, Academic Press, New York.
    • (1977) Molecular Mechanisms of Protein Biosynthesis , pp. 323-373
    • Miller, D.L.1    Weissbach, H.2
  • 2
    • 0018089806 scopus 로고
    • The role of guanosine 5-triphosphate in polypeptide elongation
    • Kaziro, Y. (1978). The role of guanosine 5-triphosphate in polypeptide elongation. Biochim. Biophys. Acta 505, 95-127.
    • (1978) Biochim. Biophys. Acta , vol.505 , pp. 95-127
    • Kaziro, Y.1
  • 3
    • 0027459639 scopus 로고
    • Recognition of tRNAs by aminoacyl-tRNA synthetases
    • Cavarelli, J. & Moras, D. (1993). Recognition of tRNAs by aminoacyl-tRNA synthetases. FASEB J. 7, 79-86.
    • (1993) FASEB J. , vol.7 , pp. 79-86
    • Cavarelli, J.1    Moras, D.2
  • 4
    • 0029608909 scopus 로고
    • Ribosomal proteins and elongation factors
    • Liljas, A. & Garber, M. (1995). Ribosomal proteins and elongation factors. Curr. Opin. Struct. Biol. 5, 721-727.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 721-727
    • Liljas, A.1    Garber, M.2
  • 5
    • 0023190457 scopus 로고
    • Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu
    • Faulhammer, H.G. & Joshi, R.L. (1987). Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu. FEBS Lett. 217, 203-211.
    • (1987) FEBS Lett. , vol.217 , pp. 203-211
    • Faulhammer, H.G.1    Joshi, R.L.2
  • 6
    • 0028219577 scopus 로고
    • Effector region of the translation elongation factor EF-Tu:GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex
    • Förster, C., Limmer, S., Zeidler, W. & Sprinzl, M. (1994). Effector region of the translation elongation factor EF-Tu:GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex. Proc. Natl. Acad. Sci. USA 91, 4254-4257.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4254-4257
    • Förster, C.1    Limmer, S.2    Zeidler, W.3    Sprinzl, M.4
  • 7
    • 0000528185 scopus 로고
    • Recognition of aminoacyl-tRNAs by protein elongation factors
    • (Söll, D. & RajBhandary, U., eds.), American Society for Microbiology Press, Washington, DC
    • Clark, B.F.C., Kjeldgaard, M., Barciszewski, J. & Sprinzl, M. (1995). Recognition of aminoacyl-tRNAs by protein elongation factors. In tRNA: Structure, Biosynthesis and Function. (Söll, D. & RajBhandary, U., eds.), pp. 423-442, American Society for Microbiology Press, Washington, DC.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 423-442
    • Clark, B.F.C.1    Kjeldgaard, M.2    Barciszewski, J.3    Sprinzl, M.4
  • 8
    • 0026556564 scopus 로고
    • A model for the aminoacyl-tRNA binding site of eukaryotic elongation factor 1α
    • Kinzy, T.G., Freeman, J.P., Johnson, A.E. & Merrick, W.C. (1992). A model for the aminoacyl-tRNA binding site of eukaryotic elongation factor 1α. J. Biol. Chem. 267, 1623-1632.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1623-1632
    • Kinzy, T.G.1    Freeman, J.P.2    Johnson, A.E.3    Merrick, W.C.4
  • 9
    • 0029958571 scopus 로고    scopus 로고
    • The GTP-binding motif - Variations on a theme
    • Kjeldgaard, M., Nyborg, J. & Clark, B.F.C. (1996). The GTP-binding motif - variations on a theme. FASEB J. 10, 1347-1368.
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 10
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A. & McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 11
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J. (1993). The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1, 35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 14
    • 0030587932 scopus 로고    scopus 로고
    • An α to β conformational switch in EF-Tu
    • Abel, K., Yoder, M.D., Hilgenfeld, R. & Jurnak, F. (1996). An α to β conformational switch in EF-Tu. Structure 4, 1153-1159.
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 15
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu:EF-Ts complex at 2.5 Å resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. & Leberman, R. (1996). The structure of the Escherichia coli EF-Tu:EF-Ts complex at 2.5 Å resolution. Nature 379, 511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 16
    • 0028895690 scopus 로고
    • Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots
    • Kjærsgaard, I.V., Knudsen, C.R. & Wiborg, O. (1995). Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots. Eur. J. Biochem. 228, 184-190.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 184-190
    • Kjærsgaard, I.V.1    Knudsen, C.R.2    Wiborg, O.3
  • 19
    • 0019872620 scopus 로고
    • Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu
    • Duffy, L., Gerber, L., Johnson, A.E. & Miller, D.L. (1981). Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu. Biochemistry 20, 4663-4666.
    • (1981) Biochemistry , vol.20 , pp. 4663-4666
    • Duffy, L.1    Gerber, L.2    Johnson, A.E.3    Miller, D.L.4
  • 20
    • 0030220858 scopus 로고    scopus 로고
    • Elongation in bacterial protein biosynthesis
    • Nyborg, J. & Kjeldgaard, M. (1996). Elongation in bacterial protein biosynthesis. Curr. Opin. Biotechnol. 7, 369-375.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 369-375
    • Nyborg, J.1    Kjeldgaard, M.2
  • 21
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7Å resolution
    • Czworkowski, J., Wang, J., Steitz, T.A. & Moore, P.B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7Å resolution. EMBO J. 13, 3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 23
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
    • Al-Karadaghi, S., Avarsson, A., Garber, M., Zheltonosova, J. & Liljas, A. (1996). The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure 4, 555-565.
    • (1996) Structure , vol.4 , pp. 555-565
    • Al-Karadaghi, S.1    Avarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 24
    • 0030091227 scopus 로고    scopus 로고
    • Protein synthesis: Imprinting through molecular mimicry
    • Liljas, A. (1996). Protein synthesis: imprinting through molecular mimicry. Curr. Biol. 6, 247-249.
    • (1996) Curr. Biol. , vol.6 , pp. 247-249
    • Liljas, A.1
  • 26
    • 0031057349 scopus 로고    scopus 로고
    • The ternary complex of EF-Tu and its role in protein biosynthesis
    • Clark, B.F.C. & Nyborg, J. (1997). The ternary complex of EF-Tu and its role in protein biosynthesis. Curr. Opin. Struct. Biol. 7, 110-116.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 110-116
    • Clark, B.F.C.1    Nyborg, J.2
  • 27
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina, M.V., Savelsbergh, A., Katunin, V.I. & Wintermeyer, W. (1997). Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385, 37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 28
    • 0030584663 scopus 로고    scopus 로고
    • A complex profile of protein elongation: Translating chemical energy into molecular movement
    • Abel, K. & Jurnak, F. (1996). A complex profile of protein elongation: translating chemical energy into molecular movement. Structure 4, 229-238.
    • (1996) Structure , vol.4 , pp. 229-238
    • Abel, K.1    Jurnak, F.2
  • 29
    • 0029563262 scopus 로고
    • Structure-based sequence alignment of elongation factor Tu and G with related GTPases involved in translation
    • Avarsson, A. (1995). Structure-based sequence alignment of elongation factor Tu and G with related GTPases involved in translation. J. Mol. Evol. 41, 1096-1104.
    • (1995) J. Mol. Evol. , vol.41 , pp. 1096-1104
    • Avarsson, A.1
  • 30
    • 0025364807 scopus 로고
    • ALMA, an editor for large sequence alignments
    • Thirup, S. & Larsen, N.E. (1990). ALMA, an editor for large sequence alignments. Proteins 7, 291-295.
    • (1990) Proteins , vol.7 , pp. 291-295
    • Thirup, S.1    Larsen, N.E.2
  • 31
    • 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
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Cowan, S., Zou, J.-Y. & Kjeldgaard, M. (1991). Improved methods for building protein 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    Cowan, S.2    Zou, J.-Y.3    Kjeldgaard, M.4


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