메뉴 건너뛰기




Volumn 8, Issue 12, 2008, Pages 4297-4306

Crystallogenesis trends of free and liganded aminoacyl-tRNA synthetases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 61549129919     PISSN: 15287483     EISSN: 15287505     Source Type: Journal    
DOI: 10.1021/cg8007766     Document Type: Conference Paper
Times cited : (15)

References (101)
  • 2
    • 33750998821 scopus 로고    scopus 로고
    • The early history of tRNA recognition by aminoacyl-tRNA synthetases
    • Giegé, R. The early history of tRNA recognition by aminoacyl-tRNA synthetases. J. Biosci. 2006, 31, 477-488.
    • (2006) J. Biosci , vol.31 , pp. 477-488
    • Giegé, R.1
  • 4
    • 0018787717 scopus 로고
    • Protein crystallization using incomplete factorial experiments
    • Carter, C. W.; Carter, C. W., Jr. Protein crystallization using incomplete factorial experiments. J. Biol. Chem. 1979, 254, 12219-12223.
    • (1979) J. Biol. Chem , vol.254 , pp. 12219-12223
    • Carter, C.W.1    Carter Jr., C.W.2
  • 5
    • 0015523222 scopus 로고
    • Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast
    • Lagerkvist, U.; Rymo, L.; Lindquist, O.; Andersson, E. Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast. J. Biol. Chem. 1972, 247, 3897-3899.
    • (1972) J. Biol. Chem , vol.247 , pp. 3897-3899
    • Lagerkvist, U.1    Rymo, L.2    Lindquist, O.3    Andersson, E.4
  • 7
    • 0000681951 scopus 로고
    • Crystallisation of trypsin-modified methionyl-tRNA synthetase from Escherichia coli
    • Waller, J.; Risler, J.; Monteilhet, C.; Zelwer, C. Crystallisation of trypsin-modified methionyl-tRNA synthetase from Escherichia coli. FEBS Lett. 1971, 16, 186-188.
    • (1971) FEBS Lett , vol.16 , pp. 186-188
    • Waller, J.1    Risler, J.2    Monteilhet, C.3    Zelwer, C.4
  • 8
    • 0014359966 scopus 로고
    • A technique for the crystallization of proteins
    • Jakoby, W. B. A technique for the crystallization of proteins. Anal. Biochem. 1968, 26, 295-298.
    • (1968) Anal. Biochem , vol.26 , pp. 295-298
    • Jakoby, W.B.1
  • 9
  • 10
    • 0035793701 scopus 로고    scopus 로고
    • How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding
    • Serre, L.; Verdon, G.; Choinowski, T.; Hervouet, N.; Risler, J.; Zelwer, C. How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding. J. Mol. Biol. 2001, 306, 863-876.
    • (2001) J. Mol. Biol , vol.306 , pp. 863-876
    • Serre, L.1    Verdon, G.2    Choinowski, T.3    Hervouet, N.4    Risler, J.5    Zelwer, C.6
  • 11
    • 0043237736 scopus 로고    scopus 로고
    • Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase
    • Crépin, T.; Schmitt, E.; Méchulam, Y.; Sampson, P. B.; Vaughan, M. D.; Honek, J. F.; Blanquet, S. Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase. J. Mol biol. 2003, 332, 59-72.
    • (2003) J. Mol biol , vol.332 , pp. 59-72
    • Crépin, T.1    Schmitt, E.2    Méchulam, Y.3    Sampson, P.B.4    Vaughan, M.D.5    Honek, J.F.6    Blanquet, S.7
  • 12
    • 0015926311 scopus 로고
    • Crystallization and preliminary x-ray diffraction studies on tyrosyl transfer RNA synthetase from Bacillus stearothermophilus
    • Reid, B.; Koch, G.; Boulanger, Y.; Hartley, B.; Blow, D. Crystallization and preliminary x-ray diffraction studies on tyrosyl transfer RNA synthetase from Bacillus stearothermophilus. J. Mol. Biol. 1973, 80, 199-201.
    • (1973) J. Mol. Biol , vol.80 , pp. 199-201
    • Reid, B.1    Koch, G.2    Boulanger, Y.3    Hartley, B.4    Blow, D.5
  • 14
    • 0035502111 scopus 로고    scopus 로고
    • Sauter, C.; Lorber, B.; Théobald-Dietrich, A.; Giegé, R. Crystallogenesis in tRNA aminoacylation systems: how packing accounts for crystallization drawbacks with yeast aspartyl-tRNA synthetase. J. Cryst. Growth 2001, 232, 399-408.
    • Sauter, C.; Lorber, B.; Théobald-Dietrich, A.; Giegé, R. Crystallogenesis in tRNA aminoacylation systems: how packing accounts for crystallization drawbacks with yeast aspartyl-tRNA synthetase. J. Cryst. Growth 2001, 232, 399-408.
  • 15
    • 0024637466 scopus 로고
    • A novel dialysis procedure for the crystallization of proteins
    • Thomas, D.; Rob, A.; Rice, D. A novel dialysis procedure for the crystallization of proteins. Protein Eng. 1989, 2, 489-491.
    • (1989) Protein Eng , vol.2 , pp. 489-491
    • Thomas, D.1    Rob, A.2    Rice, D.3
  • 16
    • 3442885098 scopus 로고    scopus 로고
    • A modified microdialysis button for use in protein crystallization
    • Lee, S.; Cudney, R. A modified microdialysis button for use in protein crystallization. J. Appl. Crystallogr. 2004, 37, 504-505.
    • (2004) J. Appl. Crystallogr , vol.37 , pp. 504-505
    • Lee, S.1    Cudney, R.2
  • 17
    • 2342596414 scopus 로고    scopus 로고
    • Genomics taken to the extreme
    • Liebl, W. Genomics taken to the extreme. Nat. Biotechnol. 2004, 22, 524-525.
    • (2004) Nat. Biotechnol , vol.22 , pp. 524-525
    • Liebl, W.1
  • 18
    • 0023646074 scopus 로고
    • Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus hb8
    • Chernaya, M. M.; Korolev, S. V.; Reshetnikova, L. S.; Safro, M. G. Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus hb8. J. Mol. Biol 1987, 198, 555-556.
    • (1987) J. Mol. Biol , vol.198 , pp. 555-556
    • Chernaya, M.M.1    Korolev, S.V.2    Reshetnikova, L.S.3    Safro, M.G.4
  • 20
    • 0028169619 scopus 로고
    • Crystallisation of the glycyl-tRNA synthetase from Thermus thermophilus and initial crystallographic data
    • Logan, D.; Cura, V.; Touzel, J.; Kern, D.; Moras, D. Crystallisation of the glycyl-tRNA synthetase from Thermus thermophilus and initial crystallographic data. J. Mol. Biol. 1994, 241, 732-735.
    • (1994) J. Mol. Biol , vol.241 , pp. 732-735
    • Logan, D.1    Cura, V.2    Touzel, J.3    Kern, D.4    Moras, D.5
  • 21
    • 0034141865 scopus 로고    scopus 로고
    • Improved crystals of Thermus thermophilus prolyl-tRNA synthetase complexed with cognate tRNA obtained by crystallization from precipitate
    • Yaremchuk, A.; Kriklivyi, I.; Cusack, S.; Tukalo, M. Improved crystals of Thermus thermophilus prolyl-tRNA synthetase complexed with cognate tRNA obtained by crystallization from precipitate. Acta Crystallogr. D Biol. Crystallogr. 2000, 56, 197-199.
    • (2000) Acta Crystallogr. D Biol. Crystallogr , vol.56 , pp. 197-199
    • Yaremchuk, A.1    Kriklivyi, I.2    Cusack, S.3    Tukalo, M.4
  • 22
    • 33744469080 scopus 로고    scopus 로고
    • Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon. Aeropyrum pernix kI
    • Iwaki, J.; Suzuki, R.; Fujimoto, Z.; Momma, M.; Kuno, A.; Hasegawa, T. Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon. Aeropyrum pernix kI. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 2005, 61, 1003-1005.
    • (2005) Acta Crystallogr. F Struct. Biol. Cryst. Commun , vol.61 , pp. 1003-1005
    • Iwaki, J.1    Suzuki, R.2    Fujimoto, Z.3    Momma, M.4    Kuno, A.5    Hasegawa, T.6
  • 23
    • 0017375692 scopus 로고
    • The amino acid sequence of tryptophanyl-tRNA synthetase from Bacillus stearothermophilus
    • Winter, G.; Hartley, B. The amino acid sequence of tryptophanyl-tRNA synthetase from Bacillus stearothermophilus. FEBS Lett. 1977, 80, 340-342.
    • (1977) FEBS Lett , vol.80 , pp. 340-342
    • Winter, G.1    Hartley, B.2
  • 24
    • 0040868504 scopus 로고
    • Tryptophanyl-tRNA synthethase of higher organisms: Enzymological, immunochemical and cytological studies
    • Kisselev, L.; Kovaleva, G. Tryptophanyl-tRNA synthethase of higher organisms: enzymological, immunochemical and cytological studies. Sov. Sci. Rev. D. Physicochem. Biol. 1987, 7, 137-186.
    • (1987) Sov. Sci. Rev. D. Physicochem. Biol , vol.7 , pp. 137-186
    • Kisselev, L.1    Kovaleva, G.2
  • 25
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublié, S.; Bricogne, G.; Gilmore, C.; Carter, C. W., Jr. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 1995, 3, 17-31.
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublié, S.1    Bricogne, G.2    Gilmore, C.3    Carter Jr., C.W.4
  • 26
    • 0015219887 scopus 로고
    • Crystallization (polymerization) of the complex of tryptophanyl-tRNA-synthetase with tryptophan
    • Kisselev, L. L.; Favorova, O. O.; Parin, A. V.; Stel'mashchuk, V.; Kisselev, N. A. Crystallization (polymerization) of the complex of tryptophanyl-tRNA-synthetase with tryptophan. Dokl. Akad. Nauk SSSR 1971, 199, 1178-1180.
    • (1971) Dokl. Akad. Nauk SSSR , vol.199 , pp. 1178-1180
    • Kisselev, L.L.1    Favorova, O.O.2    Parin, A.V.3    Stel'mashchuk, V.4    Kisselev, N.A.5
  • 27
    • 0021591726 scopus 로고
    • Crystallization of substrate and product analog complexes of tryptophanyl-tRNA synthetase
    • Carter, C. W., Jr.; Coleman, D. E. Crystallization of substrate and product analog complexes of tryptophanyl-tRNA synthetase. Fed. Proc. 1984, 43, 2981-2983.
    • (1984) Fed. Proc , vol.43 , pp. 2981-2983
    • Carter Jr., C.W.1    Coleman, D.E.2
  • 28
    • 0024038437 scopus 로고
    • Cloning heterologous genes into E. coli for enzyme production and crystal growth: Problems of expression and micro-heterogeneity
    • Carter, C. W., Jr. Cloning heterologous genes into E. coli for enzyme production and crystal growth: problems of expression and micro-heterogeneity. J. Cryst. Growth 1988, 90, 168-179.
    • (1988) J. Cryst. Growth , vol.90 , pp. 168-179
    • Carter Jr., C.W.1
  • 29
    • 0028340733 scopus 로고
    • Quantitative analysis of crystal growth. tryptophanyl-tRNA synthetase crystal polymorphism and its relationship to catalysis
    • Carter, C. W., Jr.; Doublié, S.; Coleman, D. E. Quantitative analysis of crystal growth. tryptophanyl-tRNA synthetase crystal polymorphism and its relationship to catalysis. J. Mol. Biol. 1994, 238, 346-365.
    • (1994) J. Mol. Biol , vol.238 , pp. 346-365
    • Carter Jr., C.W.1    Doublié, S.2    Coleman, D.E.3
  • 30
    • 0026206788 scopus 로고
    • Sparse matrix sampling; a screening method for crystallization of proteins
    • Jancarik, J.; Kim, S. Sparse matrix sampling; a screening method for crystallization of proteins. J. Appl. Crystallogr. 1991, 24, 409-411.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.2
  • 31
    • 12644251992 scopus 로고    scopus 로고
    • Response surface methods for optimizating and improving reproducibility of crystal growth
    • Carter, C. W., Jr. Response surface methods for optimizating and improving reproducibility of crystal growth. Methods Enzymol. 1997, 276, 74-99.
    • (1997) Methods Enzymol , vol.276 , pp. 74-99
    • Carter Jr., C.W.1
  • 32
    • 0033622155 scopus 로고    scopus 로고
    • 2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding site
    • Ilyin, V. A.; Temple, B.; Hu, M.; Li, G.; Yin, Y.; Vachette, P.; Carter, C. W. Jr. 2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site. Protein Sci. 2000, 9, 218-231.
    • (2000) Protein Sci , vol.9 , pp. 218-231
    • Ilyin, V.A.1    Temple, B.2    Hu, M.3    Li, G.4    Yin, Y.5    Vachette, P.6    Carter Jr., C.W.7
  • 33
    • 0019197641 scopus 로고
    • Cristallisation du complexe formé entre l'aspartate-tRNA de levure et son aminoacyl-tRNA synthétase spécifique.
    • Giegé, R.; Lorber, B.; Ebel, J.-P.; Moras, D.; Thierry, J.-C. Cristallisation du complexe formé entre l'aspartate-tRNA de levure et son aminoacyl-tRNA synthétase spécifique. C. R. Acad. Sc. Paris 1980, D-2 (291), 393-396.
    • (1980) C. R. Acad. Sc. Paris , vol.D-2 , Issue.291 , pp. 393-396
    • Giegé, R.1    Lorber, B.2    Ebel, J.-P.3    Moras, D.4    Thierry, J.-C.5
  • 35
    • 0021099681 scopus 로고
    • Crystallization of a tRNA-aminoacyl-tRNA synthetase complex, characterization and first crystallographic data
    • Lorber, B.; Giegé, R.; Ebel, J.-P.; Berthet, C.; Thierry, J.-C.; Moras, D. Crystallization of a tRNA-aminoacyl-tRNA synthetase complex, characterization and first crystallographic data. J. Biol. Chem. 1983, 258, 8429-8435.
    • (1983) J. Biol. Chem , vol.258 , pp. 8429-8435
    • Lorber, B.1    Giegé, R.2    Ebel, J.-P.3    Berthet, C.4    Thierry, J.-C.5    Moras, D.6
  • 36
    • 0025014522 scopus 로고
    • Stimulatory effect of ammonium sulfate at high concentrations on the aminoacylation of tRNA and tRNA-like molecules
    • Florentz, C.; Kern, D.; Giegé, R. Stimulatory effect of ammonium sulfate at high concentrations on the aminoacylation of tRNA and tRNA-like molecules. FEBS Lett. 1990, 261, 335-338.
    • (1990) FEBS Lett , vol.261 , pp. 335-338
    • Florentz, C.1    Kern, D.2    Giegé, R.3
  • 37
    • 0003009580 scopus 로고    scopus 로고
    • Nucleic acids and their complexes In Crystallization of Nucleic Acids and Proteins
    • 2nd ed, Ducruix, A. Giegé, A, Eds, IRL Press: Oxford
    • Dock-Bregeon, A.-C., Moras, D., Giegé, R. Nucleic acids and their complexes In Crystallization of Nucleic Acids and Proteins. A Practical Approach, 2nd ed.; Ducruix, A. Giegé, A., Eds.; IRL Press: Oxford, 1999, 209-243.
    • (1999) A Practical Approach , pp. 209-243
    • Dock-Bregeon, A.-C.1    Moras, D.2    Giegé, R.3
  • 40
  • 44
    • 0034705342 scopus 로고    scopus 로고
    • asp- complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain
    • asp- complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J. Mol. Biol. 2000, 299, 1313-1324.
    • (2000) J. Mol. Biol , vol.299 , pp. 1313-1324
    • Sauter, C.1    Lorber, E.2    Cavarelli, J.3    Moras, D.4    Giegé, R.5
  • 45
    • 23844499774 scopus 로고    scopus 로고
    • Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals
    • Moreno, A.; Théobald-Dietrich, A.; Lorber, B.; Sauter, C.; Giegé, R. Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals. Acta Crystallogr. D Biol. Crystallogr. 2005, 61, 789-792.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 789-792
    • Moreno, A.1    Théobald-Dietrich, A.2    Lorber, B.3    Sauter, C.4    Giegé, R.5
  • 46
    • 0003952619 scopus 로고    scopus 로고
    • Biochemical aspects and handling of macromolecular solutions and crystals
    • 2nd ed, Ducruix, A, Giegé, R, Eds, IRL Press: Oxford
    • Lorber, B., Giegé, R. Biochemical aspects and handling of macromolecular solutions and crystals. In Crystallization of Nucleic Acids and Proteins. A Practical Approach, 2nd ed.; Ducruix, A., Giegé, R., Eds.; IRL Press: Oxford, 1999; pp 17-43.
    • (1999) Crystallization of Nucleic Acids and Proteins. A Practical Approach , pp. 17-43
    • Lorber, B.1    Giegé, R.2
  • 47
    • 0026120434 scopus 로고
    • Diagnostic of protein crystallization by dynamic light scattering; an application to an aminoacyl-tRNA synthetase
    • Mikol, V.; Vincendon, P.; Eriani, G.; Hirsch, E.; Giegé, R. Diagnostic of protein crystallization by dynamic light scattering; an application to an aminoacyl-tRNA synthetase. J. Cryst. Growth 1991, 110, 195-200.
    • (1991) J. Cryst. Growth , vol.110 , pp. 195-200
    • Mikol, V.1    Vincendon, P.2    Eriani, G.3    Hirsch, E.4    Giegé, R.5
  • 48
    • 0026538086 scopus 로고
    • Pre-nucleation crystallization studies on aminoacyl-tRNA synthetases by dynamic light-scattering
    • Thibault, F.; Langowski, J.; Leberman, R. Pre-nucleation crystallization studies on aminoacyl-tRNA synthetases by dynamic light-scattering. J. Mol. Biol. 1992, 225, 185-191.
    • (1992) J. Mol. Biol , vol.225 , pp. 185-191
    • Thibault, F.1    Langowski, J.2    Leberman, R.3
  • 49
    • 35949003882 scopus 로고    scopus 로고
    • Virus-encoded aminoacyl-tRNA synthetases: Structural and functional characterization of mimivirus TyrRS and MetRS
    • Abergel, C.; Rudinger-Thirion, J.; Giegé, R.; Claverie, J. Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS. J. Virol. 2007, 81, 12406-12417.
    • (2007) J. Virol , vol.81 , pp. 12406-12417
    • Abergel, C.1    Rudinger-Thirion, J.2    Giegé, R.3    Claverie, J.4
  • 50
    • 38049086319 scopus 로고    scopus 로고
    • Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA
    • Paukstelis, P. J.; Chen, J. H.; Chase, E.; Lambowitz, A. M.; Golden, B. L. Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA. Nature 2008, 451, 94-97.
    • (2008) Nature , vol.451 , pp. 94-97
    • Paukstelis, P.J.1    Chen, J.H.2    Chase, E.3    Lambowitz, A.M.4    Golden, B.L.5
  • 52
    • 33749524376 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei
    • Yanagisawa, T.; Ishii, R.; Fukunaga, R.; Nureki, O.; Yokoyama, S. Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 2006, 62, 1031-1033.
    • (2006) Acta Crystallogr. F Struct. Biol. Cryst. Commun , vol.62 , pp. 1031-1033
    • Yanagisawa, T.1    Ishii, R.2    Fukunaga, R.3    Nureki, O.4    Yokoyama, S.5
  • 54
    • 42249114824 scopus 로고    scopus 로고
    • Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase
    • Yanagisawa, T.; Ishii, R.; Fukunaga, R.; Kobayashi, T.; Sakamoto, K.; Yokoyama, S. Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase. J. Mol. Biol. 2008, 378, 634-652.
    • (2008) J. Mol. Biol , vol.378 , pp. 634-652
    • Yanagisawa, T.1    Ishii, R.2    Fukunaga, R.3    Kobayashi, T.4    Sakamoto, K.5    Yokoyama, S.6
  • 55
    • 34249337418 scopus 로고    scopus 로고
    • Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: Crystal structure of sep-tRNA:cys-tRNA synthase from Archaeoglobus fulgidus
    • Fukunaga, R.; Yokoyama, S. Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: crystal structure of sep-tRNA:cys-tRNA synthase from Archaeoglobus fulgidus. J. Mol. Biol. 2007, 370, 128-141.
    • (2007) J. Mol. Biol , vol.370 , pp. 128-141
    • Fukunaga, R.1    Yokoyama, S.2
  • 58
    • 61549100271 scopus 로고    scopus 로고
    • Transfer RNA structure and identity In Translation Mechanisms; Lapointe, J
    • Landes Biosciences: Georgetown, TX
    • Giegé, R., Frugier, M. Transfer RNA structure and identity In Translation Mechanisms; Lapointe, J., Brakier-Gringas, L.; Landes Biosciences: Georgetown, TX, 2003; p 124.
    • (2003) Brakier-Gringas, L , pp. 124
    • Giegé, R.1    Frugier, M.2
  • 59
    • 0017121672 scopus 로고
    • The crystal structure of tyrosyl-transfer synthetase at 2.7 A resolution
    • Irwin, M.; Nyborg, J.; Reid, B.; Blow, D. The crystal structure of tyrosyl-transfer synthetase at 2.7 A resolution. J. Mol. Biol. 1976, 105, 577-586.
    • (1976) J. Mol. Biol , vol.105 , pp. 577-586
    • Irwin, M.1    Nyborg, J.2    Reid, B.3    Blow, D.4
  • 60
    • 0019953944 scopus 로고
    • Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold
    • Bhat, T.; Blow, D.; Brick, P.; Nyborg, J. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold. J. Mol. Biol. 1982, 158, 699-709.
    • (1982) J. Mol. Biol , vol.158 , pp. 699-709
    • Bhat, T.1    Blow, D.2    Brick, P.3    Nyborg, J.4
  • 61
    • 0024406896 scopus 로고
    • Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate
    • Brick, P.; Bhat, T. N.; Blow, D. M. Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. J. Mol. Biol. 1989, 208, 83-98.
    • (1989) J. Mol. Biol , vol.208 , pp. 83-98
    • Brick, P.1    Bhat, T.N.2    Blow, D.M.3
  • 62
    • 0037180444 scopus 로고    scopus 로고
    • Crystal structure of a human aminoacyl-tRNA synthetase cytokine
    • Yang, X.; Skene, R.; McRee, D.; Schimmel, P. Crystal structure of a human aminoacyl-tRNA synthetase cytokine. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 15369-15374.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 15369-15374
    • Yang, X.1    Skene, R.2    McRee, D.3    Schimmel, P.4
  • 64
    • 17744373680 scopus 로고    scopus 로고
    • Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyRS) and an engineered TyrRS specific for o-methyl-1-tyrosine
    • Zhang, Y.; Wang, L.; Schultz, P. G.; Wilson, I. A. Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyRS) and an engineered TyrRS specific for o-methyl-1-tyrosine. Protein Sci. 2005, 14, 1340-1349.
    • (2005) Protein Sci , vol.14 , pp. 1340-1349
    • Zhang, Y.1    Wang, L.2    Schultz, P.G.3    Wilson, I.A.4
  • 65
    • 0346103681 scopus 로고    scopus 로고
    • Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
    • Yang, X. L.; Otero, F. J.; Skene, R. J.; McRee, D. E.; Schimmel, P;. Ribas de Pouplana, L. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 15376-15380.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 15376-15380
    • Yang, X.L.1    Otero, F.J.2    Skene, R.J.3    McRee, D.E.4    Schimmel, P.5    Ribas de Pouplana, L.6
  • 66
    • 1542349274 scopus 로고    scopus 로고
    • Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: Insights into substrate recognition, tRNA binding, and angiogenesis activity
    • Yu, Y.; Liu, Y.; Shen, N.; Xu, X.; Xu, F.; Jia, J.; Jin, Y.; Arnold, E.; Ding, J. Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity. J. Biol. Chem. 2004, 279, 8378-8388.
    • (2004) J. Biol. Chem , vol.279 , pp. 8378-8388
    • Yu, Y.1    Liu, Y.2    Shen, N.3    Xu, X.4    Xu, F.5    Jia, J.6    Jin, Y.7    Arnold, E.8    Ding, J.9
  • 68
    • 33745794737 scopus 로고    scopus 로고
    • trp reveals the molecular basis of tRNA recognition and specificity
    • trp reveals the molecular basis of tRNA recognition and specificity. Nucleic Acids Res. 2006, 34, 3246-3258.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3246-3258
    • Shen, N.1    Guo, L.2    Yang, B.3    Jin, Y.4    Ding, J.5
  • 70
    • 34447307157 scopus 로고    scopus 로고
    • Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase
    • Yang, X. L.; Guo, M.; Kapoor, M.; Ewalt, K. L.; Otero, F. J.; Skene, R. J.; McRee, D. E.; Schimmel, P. Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase. Structure 2007, 15, 793-805.
    • (2007) Structure , vol.15 , pp. 793-805
    • Yang, X.L.1    Guo, M.2    Kapoor, M.3    Ewalt, K.L.4    Otero, F.J.5    Skene, R.J.6    McRee, D.E.7    Schimmel, P.8
  • 71
    • 84889411029 scopus 로고    scopus 로고
    • Methionyl-tRNA synthetases
    • Ibba, M, Francklyn, C, Cusack, S, Eds, Landes Bioscience: Georgetown, TX
    • Blanquet, S., Crépin, T., Mechulam, Y., Schmitt, E. Methionyl-tRNA synthetases. In The aminoacyl-tRNA synthetases; Ibba, M., Francklyn, C., Cusack, S., Eds.; Landes Bioscience: Georgetown, TX, 2005; pp 47-58.
    • (2005) The aminoacyl-tRNA synthetases , pp. 47-58
    • Blanquet, S.1    Crépin, T.2    Mechulam, Y.3    Schmitt, E.4
  • 73
    • 33845324526 scopus 로고    scopus 로고
    • Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase
    • Sekine, S.; Shichiri, M.; Bernier, S.; Chênevert, R.; Lapointe, J.; Yokoyama, S. Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Structure 2006, 14, 1791-1799.
    • (2006) Structure , vol.14 , pp. 1791-1799
    • Sekine, S.1    Shichiri, M.2    Bernier, S.3    Chênevert, R.4    Lapointe, J.5    Yokoyama, S.6
  • 75
    • 0037391084 scopus 로고    scopus 로고
    • The protein as a variable in protein crystallization
    • Dale, G. E.; Oefner, C.; D'Arcy, A. The protein as a variable in protein crystallization. J. Struct. Biol. 2003, 142, 88-97.
    • (2003) J. Struct. Biol , vol.142 , pp. 88-97
    • Dale, G.E.1    Oefner, C.2    D'Arcy, A.3
  • 76
    • 0017624847 scopus 로고
    • asp: A new high resolution x-ray diffracting crystal form of a transfer RNA
    • asp: a new high resolution x-ray diffracting crystal form of a transfer RNA. J. Mol. Biol. 1977, 115, 91-96.
    • (1977) J. Mol. Biol , vol.115 , pp. 91-96
    • Giegé, R.1    Moras, D.2    Thierry, J.3
  • 80
    • 0034658247 scopus 로고    scopus 로고
    • A domain in the n-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding
    • Frugier, M.; Moulinier, L.; Giegé, R. A domain in the n-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding. EMBO J. 2000, 19, 2371-2380.
    • (2000) EMBO J , vol.19 , pp. 2371-2380
    • Frugier, M.1    Moulinier, L.2    Giegé, R.3
  • 83
    • 0015929511 scopus 로고
    • Three dimensional structure of yeast phenylalanine transfer RNA. Folding of the polynucleotide chain
    • Kim, S.; Quigley, G.; Suddath, F.; McPherson, A.; Sneden, D.; Kim, J.; Weinzierl, J.; Rich, A. Three dimensional structure of yeast phenylalanine transfer RNA. Folding of the polynucleotide chain. Science 1973, 179, 285-288.
    • (1973) Science , vol.179 , pp. 285-288
    • Kim, S.1    Quigley, G.2    Suddath, F.3    McPherson, A.4    Sneden, D.5    Kim, J.6    Weinzierl, J.7    Rich, A.8
  • 85
    • 0001217393 scopus 로고
    • Changes of ph during biomacromolecule crystallization by vapor diffusion using ammonium sulfate as the precipitant
    • Mikol, V.; Rodeau, J.-L.; Giegé, R. Changes of ph during biomacromolecule crystallization by vapor diffusion using ammonium sulfate as the precipitant. J. Appl. Crysiallogr. 1989, 22, 155-161.
    • (1989) J. Appl. Crysiallogr , vol.22 , pp. 155-161
    • Mikol, V.1    Rodeau, J.-L.2    Giegé, R.3
  • 86
    • 0026138315 scopus 로고
    • Kinetics of pH changes in the vapor diffusion method of protein crystallization using ammonium sulfate as the precipitant
    • Rodeau, J.-L.; Mikol, V.; Giegé, R.; Lutun, P. Kinetics of pH changes in the vapor diffusion method of protein crystallization using ammonium sulfate as the precipitant. J. Appl. Crystallogr. 1991, 24, 135-141.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 135-141
    • Rodeau, J.-L.1    Mikol, V.2    Giegé, R.3    Lutun, P.4
  • 87
    • 38649092719 scopus 로고    scopus 로고
    • Handling mammalian mitochondrial tRNAs and aminoacyl-tRNA synthetases for functional and structural characterization
    • Sissler, M.; Lorber, B.; Messmer, M.; Schaller, A.; Pütz, J.; Florentz, C. Handling mammalian mitochondrial tRNAs and aminoacyl-tRNA synthetases for functional and structural characterization. Methods 2008, 44, 176-189.
    • (2008) Methods , vol.44 , pp. 176-189
    • Sissler, M.1    Lorber, B.2    Messmer, M.3    Schaller, A.4    Pütz, J.5    Florentz, C.6
  • 90
    • 0032213169 scopus 로고    scopus 로고
    • asp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. comparison with other aminoacylation systems. Acta Crystallogr. D Biol. Crystallogr. 1998, 54, 1382-1386.
    • asp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. comparison with other aminoacylation systems. Acta Crystallogr. D Biol. Crystallogr. 1998, 54, 1382-1386.
  • 91
    • 0034703763 scopus 로고    scopus 로고
    • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(val) and valyl-tRNA synthetase
    • Fukai, S.; Nureki, O.; Sekine, S.; Shimada, A.; Tao, J.; Vassylyev, D. G.; Yokoyama, S. Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(val) and valyl-tRNA synthetase. Cell 2000, 103, 793-803.
    • (2000) Cell , vol.103 , pp. 793-803
    • Fukai, S.1    Nureki, O.2    Sekine, S.3    Shimada, A.4    Tao, J.5    Vassylyev, D.G.6    Yokoyama, S.7
  • 93
    • 34548052424 scopus 로고    scopus 로고
    • Translation matters: Protein synthesis defects in inherited disease
    • Scheper, G. C.; van der Knaap, M. S.; Proud, C. G. Translation matters: protein synthesis defects in inherited disease. Nat. Rev. Genet. 2007, 8, 711-723.
    • (2007) Nat. Rev. Genet , vol.8 , pp. 711-723
    • Scheper, G.C.1    van der Knaap, M.S.2    Proud, C.G.3
  • 94
    • 36549057813 scopus 로고    scopus 로고
    • McPherson, A, Giegé, R. Crystallogenesis research for biology in the last two decades as seen from the international conferences on the crystallization of biological macromolecules
    • McPherson, A.; Giegé, R. Crystallogenesis research for biology in the last two decades as seen from the international conferences on the crystallization of biological macromolecules. Cryst. Growth Des. 2007, 7, 2126-2133.
    • (2007) Cryst. Growth Des , vol.7 , pp. 2126-2133
  • 95
    • 0035071488 scopus 로고    scopus 로고
    • Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermits thermophilus aspartyl-tRNA synthetase-1
    • Zhu, D.-W.; Lorber, B.; Sauter, C.; Ng, J. D.; Bénas, P; Grimellec, C.; Le, C.; Giegé, R. Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermits thermophilus aspartyl-tRNA synthetase-1. Acta Crystallogr. D Biol. Crystallogr. 2001, 57, 552-558.
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 552-558
    • Zhu, D.-W.1    Lorber, B.2    Sauter, C.3    Ng, J.D.4    Bénas, P.5    Grimellec, C.6    Le, C.7    Giegé, R.8
  • 96
    • 0030565904 scopus 로고    scopus 로고
    • The crystallization of macromolecules from precipitates: Evidence for ostwald ripening
    • Ng, J. D.; Lorber, B.; Witz, J.; Théobald-Dietrich, A.; Kern, D.; Giegé, R. The crystallization of macromolecules from precipitates: evidence for ostwald ripening. J. Cryst. Growth 1996, 168, 50-62.
    • (1996) J. Cryst. Growth , vol.168 , pp. 50-62
    • Ng, J.D.1    Lorber, B.2    Witz, J.3    Théobald-Dietrich, A.4    Kern, D.5    Giegé, R.6
  • 97
    • 0036005618 scopus 로고    scopus 로고
    • Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: Space-grown crystals are more useful for structural determination
    • Ng, J. D.; Sauter, C.; Lorber, B.; Kirkland, N.; Arnez, J.; Giegé, R. Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 645-652.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 645-652
    • Ng, J.D.1    Sauter, C.2    Lorber, B.3    Kirkland, N.4    Arnez, J.5    Giegé, R.6
  • 98
    • 0036793551 scopus 로고    scopus 로고
    • From conventional crystallization to better crystals from space: A review on pilot crystallogenesis studies with aspartyl-tRNA synthetase
    • Lorber, B.; Théobald-Dietrich, A.; Charron, C.; Sauter, C.; Ng, J. D.; Zhu, D.-W.; Giegé, R. From conventional crystallization to better crystals from space: a review on pilot crystallogenesis studies with aspartyl-tRNA synthetase. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 1674-1680.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1674-1680
    • Lorber, B.1    Théobald-Dietrich, A.2    Charron, C.3    Sauter, C.4    Ng, J.D.5    Zhu, D.-W.6    Giegé, R.7
  • 99
    • 0033516411 scopus 로고    scopus 로고
    • Characterization of protein and virus crystals by quasi-planar wave X-ray topography: A comparison between crystals grown in solution and in agarose gel
    • Lorber, B.; Sauter, C.; Ng, J. D.; Zhu, D.-W.; Giegé, R.; Vidal, O.; Robert, M.-C.; Capelle, B. Characterization of protein and virus crystals by quasi-planar wave X-ray topography: a comparison between crystals grown in solution and in agarose gel. J. Cryst. Growth 1999, 204, 357-368.
    • (1999) J. Cryst. Growth , vol.204 , pp. 357-368
    • Lorber, B.1    Sauter, C.2    Ng, J.D.3    Zhu, D.-W.4    Giegé, R.5    Vidal, O.6    Robert, M.-C.7    Capelle, B.8
  • 100
    • 0036615179 scopus 로고    scopus 로고
    • The biological macromolecule crystallization database: Crystallization procedures and strategies
    • Gilliland, G. L.; Tung, M.; Ladner, J. E. The biological macromolecule crystallization database: crystallization procedures and strategies. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 916-920.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 916-920
    • Gilliland, G.L.1    Tung, M.2    Ladner, J.E.3
  • 101
    • 33750336348 scopus 로고    scopus 로고
    • MPCD: A new interactive online crystallization data bank for screening strategies
    • Charles, M.; Veesler, S.; Bonneté, F. MPCD: a new interactive online crystallization data bank for screening strategies. Acta Crystallogr. D Biol. Crystallogr. 2006, 62, 1311-1318.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 1311-1318
    • Charles, M.1    Veesler, S.2    Bonneté, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.