메뉴 건너뛰기




Volumn 412, Issue 3, 2011, Pages 437-452

Crystal structure of the archaeal asparagine synthetase: Interrelation with aspartyl-tRNA and asparaginyl-tRNA synthetases

Author keywords

aminoacyl tRNA synthetase; asparagine synthesis; asparagine synthetase; evolution

Indexed keywords

ASPARAGINE; ASPARAGINYL TRANSFER RIBONUCLEIC ACID SYNTHETASE; ASPARTATE AMMONIA LIGASE; ASPARTATE TRANSFER RNA LIGASE; ASPARTIC ACID; LIGASE; UNCLASSIFIED DRUG;

EID: 80052349173     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.050     Document Type: Article
Times cited : (11)

References (33)
  • 2
    • 0018595061 scopus 로고
    • The twenty aminoacyl-tRNA synthetases from Escherichia coli. General separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities
    • Kern D., and Lapointe J. The twenty aminoacyl-tRNA synthetases from Escherichia coli. General separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities Biochimie 61 1979 1257 1272 (Pubitemid 10115620)
    • (1979) Biochimie , vol.61 , Issue.11-12 , pp. 1257-1272
    • Kern, D.1    Lapointe, J.2
  • 3
    • 0017376956 scopus 로고
    • The yeast aminoacyl tRNA synthetases. Methodology for their complete or partial purification and comparison of their relative activities under various extraction conditions
    • Kern D., Dietrich A., Fasiolo F., Renaud M., Giegé R., and Ebel J.P. The yeast aminoacyl-tRNA synthetases. Methodology for their complete or partial purification and comparison of their relative activities under various extraction conditions Biochimie 59 1977 453 462 (Pubitemid 8142761)
    • (1977) Biochimie , vol.59 , Issue.5-6 , pp. 453-462
    • Kern, D.1    Dietrich, A.2    Fasiolo, F.3
  • 4
    • 0029039915 scopus 로고
    • Comparison of the enzymatic properties of the two Escherichia coli lysyl-tRNA synthetase species
    • Brevet A., Chen J., Lévêque F., Blanquet S., and Plateau P. Comparison of the enzymatic properties of the two Escherichia coli lysyl-tRNA synthetase species J. Biol. Chem. 270 1995 14439 14444
    • (1995) J. Biol. Chem. , vol.270 , pp. 14439-14444
    • Brevet, A.1    Chen, J.2    Lévêque, F.3    Blanquet, S.4    Plateau, P.5
  • 5
    • 11144357971 scopus 로고    scopus 로고
    • Aminoacyl-tRNAs: Setting the limits of the genetic code
    • DOI 10.1101/gad.1187404
    • Ibba M., and Söll D. Aminoacyl-tRNAs: setting the limits of the genetic code Genes Dev. 18 2004 731 738 (Pubitemid 38480885)
    • (2004) Genes and Development , vol.18 , Issue.7 , pp. 731-738
    • Ibba, M.1    Soll, D.2
  • 6
    • 33746940908 scopus 로고    scopus 로고
    • Asparaginyl-tRNA synthetase: Pathway and evolutionary history of tRNA asparaginylation
    • M. Ibba, C. Francklyn, S. Cusack, Landes Bioscience Georgetown, TX chapt. 20
    • Kern D., Roy H., and Becker H.D. Asparaginyl-tRNA synthetase: pathway and evolutionary history of tRNA asparaginylation M. Ibba, C. Francklyn, S. Cusack, The Aminoacyl-tRNA Synthetases 2005 Landes Bioscience Georgetown, TX chapt. 20
    • (2005) The Aminoacyl-tRNA Synthetases
    • Kern, D.1    Roy, H.2    Becker, H.D.3
  • 9
    • 0029781454 scopus 로고    scopus 로고
    • tRNA-dependent asparagine formation
    • Curnow A.W., Ibba M., and Söll D. tRNA-dependent asparagine formation Nature 382 1996 589 590 (Pubitemid 26268945)
    • (1996) Nature , vol.382 , Issue.6592 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Soll, D.3
  • 11
    • 0014670438 scopus 로고
    • The asparagine synthetase of Escherichia coli: I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products
    • Cedar H., and Schwartz J.H. The asparagine synthetase of Escherichia coli: I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products J. Biol. Chem. 244 1969 4112 4121
    • (1969) J. Biol. Chem. , vol.244 , pp. 4112-4121
    • Cedar, H.1    Schwartz, J.H.2
  • 12
    • 0014670428 scopus 로고
    • The asparagine synthetase of Escherichia coli: II. Studies on mechanism
    • Cedar H., and Schwartz J.H. The asparagine synthetase of Escherichia coli: II. Studies on mechanism J. Biol. Chem. 244 1969 4122 4127
    • (1969) J. Biol. Chem. , vol.244 , pp. 4122-4127
    • Cedar, H.1    Schwartz, J.H.2
  • 13
    • 0026468562 scopus 로고
    • An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase
    • Richards N.G., and Schuster S.M. An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase FEBS Lett. 313 1992 98 102
    • (1992) FEBS Lett. , vol.313 , pp. 98-102
    • Richards, N.G.1    Schuster, S.M.2
  • 14
    • 0014643835 scopus 로고
    • Gln as an intermediate in Bacillus subtilis glutaminyl-tRNA synthesis
    • Gln as an intermediate in Bacillus subtilis glutaminyl-tRNA synthesis Cold Spring Harb. Symp. Quant. Biol. 34 1969 521 528
    • (1969) Cold Spring Harb. Symp. Quant. Biol. , vol.34 , pp. 521-528
    • Wilcox, M.1
  • 15
    • 0031984643 scopus 로고    scopus 로고
    • Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase
    • DOI 10.1038/nsb0198-15
    • Nakatsu T., Kato H., and Oda J. Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetases Nat. Struct. Biol. 5 1998 15 19 (Pubitemid 28048970)
    • (1998) Nature Structural Biology , vol.5 , Issue.1 , pp. 15-19
    • Nakatsu, T.1    Kato, H.2    Oda, J.3
  • 18
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G., Delarue M., Poch O., Gangloff J., and Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs Nature 347 1990 203 206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 19
    • 0032169440 scopus 로고    scopus 로고
    • Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: Archaeon specificity and catalytic mechanism of adenylate formation
    • DOI 10.1093/emboj/17.17.5227
    • Schmitt E., Moulinier L., Fujiwara S., Imanaka T., Thierry J.C., and Moras D. Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation EMBO J. 17 1998 5227 5237 (Pubitemid 28408488)
    • (1998) EMBO Journal , vol.17 , Issue.17 , pp. 5227-5237
    • Schmitt, E.1    Moulinier, L.2    Fujiwara, S.3    Imanaka, T.4    Thierry, J.-C.5    Moras, D.6
  • 20
    • 33746752845 scopus 로고    scopus 로고
    • Structural Basis of the Water-assisted Asparagine Recognition by Asparaginyl-tRNA Synthetase
    • DOI 10.1016/j.jmb.2006.04.068, PII S0022283606005614
    • Iwasaki W., Sekine S., Kuroishi C., Kuramitsu S., Shirouzu M., and Yokoyama S. Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase J. Mol. Biol. 360 2006 329 342 (Pubitemid 44202311)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.2 , pp. 329-342
    • Iwasaki, W.1    Sekine, S.-i.2    Kuroishi, C.3    Kuramitsu, S.4    Shirouzu, M.5    Yokoyama, S.6
  • 21
    • 79251595309 scopus 로고    scopus 로고
    • A hybrid structural model of the complete Brugia malayi cytoplasmic asparaginyl-tRNA synthetase
    • Crépin T., Peterson F., Häertlein M., Jensen D., Wang C., Cusack S., and Kron M. A hybrid structural model of the complete Brugia malayi cytoplasmic asparaginyl-tRNA synthetase J. Mol. Biol. 405 2011 1056 1069
    • (2011) J. Mol. Biol. , vol.405 , pp. 1056-1069
    • Crépin, T.1    Peterson, F.2    Häertlein, M.3    Jensen, D.4    Wang, C.5    Cusack, S.6    Kron, M.7
  • 22
    • 0032525301 scopus 로고    scopus 로고
    • The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: The mechanism of discrimination between asparagine and aspartic acid
    • Berthet-Colominas C., Seignovert L., Härtlein M., Grotli M., Cusack S., and Leberman R. The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid EMBO J. 17 1998 2947 2960
    • (1998) EMBO J. , vol.17 , pp. 2947-2960
    • Berthet-Colominas, C.1    Seignovert, L.2    Härtlein, M.3    Grotli, M.4    Cusack, S.5    Leberman, R.6
  • 23
    • 0027860348 scopus 로고
    • Yeast aspartyl-tRNA synthetase: A structural view of the aminoacylation reaction
    • DOI 10.1016/0300-9084(93)90011-G
    • Cavarelli J., Rees B., Thierry J.C., and Moras D. Yeast aspartyl-tRNA synthetase: a structural view of the aminoacylation reaction Biochimie 75 1993 1117 1123 (Pubitemid 24089074)
    • (1993) Biochimie , vol.75 , Issue.12 , pp. 1117-1123
    • Cavarelli, J.1    Rees, B.2    Thierry, J.C.3    Moras, D.4
  • 26
    • 77956871565 scopus 로고    scopus 로고
    • Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation
    • Blaise M., Bailly M., Fréchin M., Behrens M.A., Fischer F., and Oliveira C.L. Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation EMBO J. 29 2010 3118 3129
    • (2010) EMBO J. , vol.29 , pp. 3118-3129
    • Blaise, M.1    Bailly, M.2    Fréchin, M.3    Behrens, M.A.4    Fischer, F.5    Oliveira, C.L.6
  • 28
    • 16544388164 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction data of an archaeal asparagine synthetase related to asparaginyl-tRNA synthetase
    • DOI 10.1107/S0907444904003117
    • Charron C., Roy H., Blaise M., Giegé R., and Kern D. Crystallization and preliminary X-ray diffraction data of an archaeal asparagine synthetase related to asparaginyl-tRNA synthetase Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 2004 767 769 (Pubitemid 41184842)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.4 , pp. 767-769
    • Charron, C.1    Roy, H.2    Blaise, M.3    Giege, R.4    Kern, D.5
  • 29
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch W. Integration, scaling, space-group assignment and post-refinement Acta Crystallogr., Sect. D: Biol. Crystallogr. 66 2010 133 144
    • (2010) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.