메뉴 건너뛰기




Volumn 145, Issue 5, 2009, Pages 555-563

Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: Insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate

Author keywords

Aminoacyl tRNA synthetase; Crystal structure; L lysine hydroxamate; Lysyl tRNA synthetase; Seryl tRNA synthetase

Indexed keywords

ADENOSINE PHOSPHATE; ENZYME; LEVO LYSINE HYDROXAMATE; LYSINE TRANSFER RNA LIGASE; LYSYLADENYLATE; UNCLASSIFIED DRUG;

EID: 66749189601     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp014     Document Type: Article
Times cited : (13)

References (23)
  • 1
    • 0042213065 scopus 로고
    • Specialty in protein synthesis
    • Berg, P. (1961) Specialty in protein synthesis. Annu. Rev. Biochem. 30, 293-322
    • (1961) Annu. Rev. Biochem , vol.30 , pp. 293-322
    • Berg, P.1
  • 2
    • 0017230165 scopus 로고
    • Mechanism of aminoacylation of tRNA. Proof of the aminocyl adenylate pathway for the isoleucyl- and tyrosyl- tRNA synthetase form Escherichia coli K12
    • Fersht, A.R. and Kaethner, M.M. (1976) Mechanism of aminoacylation of tRNA. Proof of the aminocyl adenylate pathway for the isoleucyl- and tyrosyl- tRNA synthetase form Escherichia coli K12. Biochemistry 15, 818-823
    • (1976) Biochemistry , vol.15 , pp. 818-823
    • Fersht, A.R.1    Kaethner, M.M.2
  • 3
    • 0025158208 scopus 로고
    • Partition of tRNA syntheases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J., and Moras, D. (1990) Partition of tRNA syntheases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 4
    • 0034713835 scopus 로고    scopus 로고
    • Active site of lysyl-tRNA synthetase: Structural studies of the adenylation reaction
    • Desogus, G., Todone, F., Brick, P., and Onesti, S. (2000) Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction. Biochemistry 39, 8418-8425
    • (2000) Biochemistry , vol.39 , pp. 8418-8425
    • Desogus, G.1    Todone, F.2    Brick, P.3    Onesti, S.4
  • 5
    • 0034710994 scopus 로고    scopus 로고
    • Structural studies of lysyl-tRNA synthetase: Conformational changes induced by substrate binding
    • Onesti, S., Desogus, G., Brevet, A., Chen, J., Plateau, P., Blanquet, S., and Brick, P. (2000) Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry 39, 12853-12861
    • (2000) Biochemistry , vol.39 , pp. 12853-12861
    • Onesti, S.1    Desogus, G.2    Brevet, A.3    Chen, J.4    Plateau, P.5    Blanquet, S.6    Brick, P.7
  • 6
    • 0029876477 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase from Bacillus stearothermophilus. Purification, and fluorometric and kinetic analysis of the binding of substrates, L-lysine and ATP
    • Takita, T., Ohkubo, Y., Shima, H., Muto, T., Shimizu, N., Sukata, T., Ito, H., Saito, Y., Inouye, K., Hiromi, K., and Tonomura, B. (1996) Lysyl-tRNA synthetase from Bacillus stearothermophilus. Purification, and fluorometric and kinetic analysis of the binding of substrates, L-lysine and ATP. J. Biochem. 119, 680-689
    • (1996) J. Biochem , vol.119 , pp. 680-689
    • Takita, T.1    Ohkubo, Y.2    Shima, H.3    Muto, T.4    Shimizu, N.5    Sukata, T.6    Ito, H.7    Saito, Y.8    Inouye, K.9    Hiromi, K.10    Tonomura, B.11
  • 7
    • 0031053043 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase from Bacillus stearothermophilus. Formation and isolation of the enzyme·lysyladenylate complex and its analogue
    • Takita, T., Hashimoto, S., Ohkubo, Y., Muto, T., Shimizu, N., Sukata, T., Inouye, K., Hiromi, K., and Tonomura, B. (1997) Lysyl-tRNA synthetase from Bacillus stearothermophilus. Formation and isolation of the enzyme·lysyladenylate complex and its analogue. J. Biochem. 121, 244-250
    • (1997) J. Biochem , vol.121 , pp. 244-250
    • Takita, T.1    Hashimoto, S.2    Ohkubo, Y.3    Muto, T.4    Shimizu, N.5    Sukata, T.6    Inouye, K.7    Hiromi, K.8    Tonomura, B.9
  • 8
    • 0031872794 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase fro m Bacillus stearothermophilus. Stopped-flow kinetic anaLysis of enzyme·lysyladenylate formation
    • Takita, T., Akita, E., Inouye, K., and Tonomura, B. (1998) Lysyl-tRNA synthetase fro m Bacillus stearothermophilus. Stopped-flow kinetic anaLysis of enzyme·lysyladenylate formation. J. Biochem. 124, 45-50
    • (1998) J. Biochem , vol.124 , pp. 45-50
    • Takita, T.1    Akita, E.2    Inouye, K.3    Tonomura, B.4
  • 10
    • 0037462877 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase from Bacillus stearothermophilus: The Trp314 residue is shielded in a non-polar environment and is responsible for the fluorescence changes observed in the amino acid activation reaction
    • Takita, T., Nakagoshi, M., Inouye, K., and Tonomura, B. (2003) Lysyl-tRNA synthetase from Bacillus stearothermophilus: the Trp314 residue is shielded in a non-polar environment and is responsible for the fluorescence changes observed in the amino acid activation reaction. J. Mol. Biol. 325, 677-695
    • (2003) J. Mol. Biol , vol.325 , pp. 677-695
    • Takita, T.1    Nakagoshi, M.2    Inouye, K.3    Tonomura, B.4
  • 11
    • 0037047427 scopus 로고    scopus 로고
    • Transition state stabilization by the N-terminal anticodon-binding domain of lysyl-tRNA synthetase
    • Takita, T. and Inouye, K. (2002) Transition state stabilization by the N-terminal anticodon-binding domain of lysyl-tRNA synthetase. J. Biol. Chem. 277, 29275-29282
    • (2002) J. Biol. Chem , vol.277 , pp. 29275-29282
    • Takita, T.1    Inouye, K.2
  • 12
    • 0342647021 scopus 로고    scopus 로고
    • Characterization of yeast seryl-tRNA synthetase active site mutants with improved discrimination against substrate analogues
    • Landeka, I., Filipic-Rocak, S., Zinic, B., and Weygand-Durasevic, I. (2000) Characterization of yeast seryl-tRNA synthetase active site mutants with improved discrimination against substrate analogues. Biochim. Biophys. Acta 1480, 160-170
    • (2000) Biochim. Biophys. Acta , vol.1480 , pp. 160-170
    • Landeka, I.1    Filipic-Rocak, S.2    Zinic, B.3    Weygand-Durasevic, I.4
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG - a tool for high-throughput crystallography of protein-ligand complexes
    • Schüettelkopf, A.W. and van Aalten, D.M.F. (2004) PRODRG - a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. Sect. D 60, 1355-1363
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 1355-1363
    • Schüettelkopf, A.W.1    van Aalten, D.M.F.2
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 0028057108 scopus 로고    scopus 로고
    • Merrit, E.A. and Murphy, M.E.P, 1994 Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. Sect. D. 50, 869-873
    • Merrit, E.A. and Murphy, M.E.P. (1994) Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. Sect. D. 50, 869-873
  • 19
    • 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. Graph. Model. 15, 132-134
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 20
    • 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. Graph. Model. 15, 112-113
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 112-113
    • Esnouf, R.M.1
  • 21
    • 2342441329 scopus 로고    scopus 로고
    • Divergence in noncognate amino acid recognition between class I and class II lysyl-tRNA synthetases
    • Levengood, J., Ataide, S.F., Roy, H., and Ibba, M. (2004) Divergence in noncognate amino acid recognition between class I and class II lysyl-tRNA synthetases. J. Biol. Chem. 279, 17707-17714
    • (2004) J. Biol. Chem , vol.279 , pp. 17707-17714
    • Levengood, J.1    Ataide, S.F.2    Roy, H.3    Ibba, M.4
  • 22
    • 9644265294 scopus 로고    scopus 로고
    • Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogues
    • Berneir, S., Akochy, P.-M., Lapointe, J., and Chenevert, R. (2005) Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogues. Bioorg. Med. Chem. 13, 69-75
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 69-75
    • Berneir, S.1    Akochy, P.-M.2    Lapointe, J.3    Chenevert, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.