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Volumn 6, Issue 1, 1998, Pages 101-108

tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase

Author keywords

Anticodon; Class IIa synthetase; Genetic code; Prolyl tRNA synthetase; Protein RNA recognition; tRNA

Indexed keywords

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 0032518606     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00011-2     Document Type: Article
Times cited : (82)

References (23)
  • 1
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack, S. (1995). Eleven down and nine to go. Nat. Struct. Biol. 2, 824-831.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 2
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez, J.G. & Moras, D. (1997). Structural and functional considerations of the aminoacylation reaction. Trends Biochem.Sci. 22, 189-232.
    • (1997) Trends Biochem.Sci. , vol.22 , pp. 189-232
    • Arnez, J.G.1    Moras, D.2
  • 3
    • 0025874160 scopus 로고
    • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases
    • Cusack, S., Härtlein, M. & Leberman, R. (1991). Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucl. Acids Res. 19, 3489-3498.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3489-3498
    • Cusack, S.1    Härtlein, M.2    Leberman, R.3
  • 4
    • 0027851759 scopus 로고
    • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: An update
    • Cusack, S. (1993). Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update. Biochimie. 75, 1077-1081.
    • (1993) Biochimie , vol.75 , pp. 1077-1081
    • Cusack, S.1
  • 6
    • 0029091055 scopus 로고
    • Crystal structure of glycyl-tRNA synthetase from T. thermophilus
    • Logan, D.T., Mazauric, M.-H., Kern, D. & Moras, D. (1995). Crystal structure of glycyl-tRNA synthetase from T. thermophilus. EMBO J. 14, 4156-4167.
    • (1995) EMBO J. , vol.14 , pp. 4156-4167
    • Logan, D.T.1    Mazauric, M.-H.2    Kern, D.3    Moras, D.4
  • 7
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from E. coli complexed with histidyl-adenylate
    • Arnez, J.G., Harris, D.C., Mitschler, A., Rees, B., Francklyn, C.S. & Moras, D. (1995) Crystal structure of histidyl-tRNA synthetase from E. coli complexed with histidyl-adenylate. EMBO J. 14, 4143-4155.
    • (1995) EMBO J. , vol.14 , pp. 4143-4155
    • Arnez, J.G.1    Harris, D.C.2    Mitschler, A.3    Rees, B.4    Francklyn, C.S.5    Moras, D.6
  • 8
    • 0030934790 scopus 로고    scopus 로고
    • Crystal structure analysis of activation of histidine by T. thermophilus histidyl-tRNA synthetase
    • Åberg, A., Yaremchuk, A., Tukalo, M., Rasmussen, B. & Cusack, S. (1997). Crystal structure analysis of activation of histidine by T. thermophilus histidyl-tRNA synthetase. Biochemistry 36, 3084-3094.
    • (1997) Biochemistry , vol.36 , pp. 3084-3094
    • Åberg, A.1    Yaremchuk, A.2    Tukalo, M.3    Rasmussen, B.4    Cusack, S.5
  • 9
    • 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
  • 11
    • 0029907152 scopus 로고    scopus 로고
    • lys transcript: Anti-codon recognition and conformational changes upon binding of a lysyladenylate analogue
    • lys transcript: anti-codon recognition and conformational changes upon binding of a lysyladenylate analogue. EMBO J. 15, 6321-6334.
    • (1996) EMBO J. , vol.15 , pp. 6321-6334
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 13
    • 0028983874 scopus 로고
    • thr towards S. cerevisiae threonyl-tRNA synthetase
    • thr towards S. cerevisiae threonyl-tRNA synthetase. Nucl. Acids Res. 23, 2831-2836.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2831-2836
    • Nameki, N.1
  • 15
    • 0027436686 scopus 로고
    • An operational RNA code for amino acids and possible relationship to genetic code
    • Schimmel, P., Geigé, R., Moras, D. & Yokoyama, S. (1993). An operational RNA code for amino acids and possible relationship to genetic code. Proc. Natl. Acad. Sci. USA 90, 8736-8768.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8736-8768
    • Schimmel, P.1    Geigé, R.2    Moras, D.3    Yokoyama, S.4
  • 16
    • 0028943076 scopus 로고
    • Structure, function and evolution of seryl-tRNA synthetases: Implications for the evolution of aminoacyltRNA synthetases and the genetic code
    • Härtlein, M. & Cusack, S. (1995). Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyltRNA synthetases and the genetic code. J. Mol. Evol. 40, 519-530.
    • (1995) J. Mol. Evol. , vol.40 , pp. 519-530
    • Härtlein, M.1    Cusack, S.2
  • 18
    • 0028237043 scopus 로고
    • Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA synthetase in E. coli
    • Yan, W. & Francklyn, C. (1994). Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA synthetase in E. coli. J. Biol. Chem. 269, 10022-10027.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10022-10027
    • Yan, W.1    Francklyn, C.2
  • 19
    • 0026525771 scopus 로고
    • Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs
    • Francklyn, C., Musier-Forsyth, K. & Schimmel, P. (1992). Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs. Eur. J. Biochem. 206, 315-321.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 315-321
    • Francklyn, C.1    Musier-Forsyth, K.2    Schimmel, P.3
  • 21
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • 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
  • 22
    • 0003769049 scopus 로고
    • Yale University. Press, New Haven, CT, USA
    • Brünger, T.A. (1992). X-PLOR version 3.1. Yale University. Press, New Haven, CT, USA.
    • (1992) X-PLOR Version 3.1
    • Brünger, T.A.1
  • 23
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MOLSCRIPT that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). An extensively modified version of MOLSCRIPT that includes greatly enhanced coloring capabilities J. Mol. Graphics, 15, 133-138.
    • (1997) J. Mol. Graphics , vol.15 , pp. 133-138
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.