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Volumn 21, Issue 11, 2013, Pages 2078-2086

Crystal structure of human seryl-tRNA synthetase and Ser-SA complex reveals a molecular lever specific to higher eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

5' O [N (SERYL)SULFAMOYL]ADENOSINE; ADENOSINE DERIVATIVE; SERINE TRANSFER RNA LIGASE; SYNTHETASE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84887404590     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.08.021     Document Type: Article
Times cited : (22)

References (32)
  • 4
    • 34447308200 scopus 로고    scopus 로고
    • A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities
    • K. Beebe, W. Waas, Z. Druzina, M. Guo, and P. Schimmel A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities Anal. Biochem. 368 2007 111 121
    • (2007) Anal. Biochem. , vol.368 , pp. 111-121
    • Beebe, K.1    Waas, W.2    Druzina, Z.3    Guo, M.4    Schimmel, P.5
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 0345436050 scopus 로고    scopus 로고
    • Selenocysteine inserting tRNAs: An overview
    • S. Commans, and A. Böck Selenocysteine inserting tRNAs: an overview FEMS Microbiol. Rev. 23 1999 335 351
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 335-351
    • Commans, S.1    Böck, A.2
  • 10
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A
    • S. Cusack, C. Berthet-Colominas, M. Härtlein, N. Nassar, and R. Leberman A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A Nature 347 1990 249 255
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 11
    • 0025874160 scopus 로고
    • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases
    • S. Cusack, M. Härtlein, and R. Leberman Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases Nucleic Acids Res. 19 1991 3489 3498
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3489-3498
    • Cusack, S.1    Härtlein, M.2    Leberman, R.3
  • 12
    • 0030011019 scopus 로고    scopus 로고
    • The crystal structure of the ternary complex of T thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site
    • S. Cusack, A. Yaremchuk, and M. Tukalo The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site EMBO J. 15 1996 2834 2842
    • (1996) EMBO J. , vol.15 , pp. 2834-2842
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 14
    • 84863357487 scopus 로고    scopus 로고
    • TRNA-controlled nuclear import of a human tRNA synthetase
    • G. Fu, T. Xu, Y. Shi, N. Wei, and X.L. Yang tRNA-controlled nuclear import of a human tRNA synthetase J. Biol. Chem. 287 2012 9330 9334
    • (2012) J. Biol. Chem. , vol.287 , pp. 9330-9334
    • Fu, G.1    Xu, T.2    Shi, Y.3    Wei, N.4    Yang, X.L.5
  • 15
    • 0027491528 scopus 로고
    • Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution
    • M. Fujinaga, C. Berthet-Colominas, A.D. Yaremchuk, M.A. Tukalo, and S. Cusack Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution J. Mol. Biol. 234 1993 222 233
    • (1993) J. Mol. Biol. , vol.234 , pp. 222-233
    • Fujinaga, M.1    Berthet-Colominas, C.2    Yaremchuk, A.D.3    Tukalo, M.A.4    Cusack, S.5
  • 16
    • 67649891971 scopus 로고    scopus 로고
    • Noncanonical activity of seryl-tRNA synthetase is involved in vascular development
    • H. Fukui, R. Hanaoka, and A. Kawahara Noncanonical activity of seryl-tRNA synthetase is involved in vascular development Circ. Res. 104 2009 1253 1259
    • (2009) Circ. Res. , vol.104 , pp. 1253-1259
    • Fukui, H.1    Hanaoka, R.2    Kawahara, A.3
  • 17
    • 0032524029 scopus 로고    scopus 로고
    • (Sec) substrates for human seryl-tRNA synthetase: Contribution of tRNA domains to serylation and tertiary structure
    • (Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure FEBS Lett. 427 1998 315 319
    • (1998) FEBS Lett. , vol.427 , pp. 315-319
    • Heckl, M.1    Busch, K.2    Gross, H.J.3
  • 18
    • 67649882602 scopus 로고    scopus 로고
    • Genetic evidence for a noncanonical function of seryl-tRNA synthetase in vascular development
    • W. Herzog, K. Müller, J. Huisken, and D.Y. Stainier Genetic evidence for a noncanonical function of seryl-tRNA synthetase in vascular development Circ. Res. 104 2009 1260 1266
    • (2009) Circ. Res. , vol.104 , pp. 1260-1266
    • Herzog, W.1    Müller, K.2    Huisken, J.3    Stainier, D.Y.4
  • 19
    • 62449208889 scopus 로고    scopus 로고
    • Crystallographic and mutational studies of seryl-tRNA synthetase from the archaeon Pyrococcus horikoshii
    • Y. Itoh, S. Sekine, C. Kuroishi, T. Terada, M. Shirouzu, S. Kuramitsu, and S. Yokoyama Crystallographic and mutational studies of seryl-tRNA synthetase from the archaeon Pyrococcus horikoshii RNA Biol. 5 2008 169 177
    • (2008) RNA Biol. , vol.5 , pp. 169-177
    • Itoh, Y.1    Sekine, S.2    Kuroishi, C.3    Terada, T.4    Shirouzu, M.5    Kuramitsu, S.6    Yokoyama, S.7
  • 20
    • 0025878603 scopus 로고
    • Escherichia coli seryl-tRNA synthetase: The structure of a class 2 aminoacyl-tRNA synthetase
    • R. Leberman, M. Härtlein, and S. Cusack Escherichia coli seryl-tRNA synthetase: the structure of a class 2 aminoacyl-tRNA synthetase Biochim. Biophys. Acta 1089 1991 287 298
    • (1991) Biochim. Biophys. Acta , vol.1089 , pp. 287-298
    • Leberman, R.1    Härtlein, M.2    Cusack, S.3
  • 23
    • 0026625691 scopus 로고
    • Eight base changes are sufficient to convert a leucine-inserting tRNA into a serine-inserting tRNA
    • J. Normanly, T. Ollick, and J. Abelson Eight base changes are sufficient to convert a leucine-inserting tRNA into a serine-inserting tRNA Proc. Natl. Acad. Sci. USA 89 1992 5680 5684
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5680-5684
    • Normanly, J.1    Ollick, T.2    Abelson, J.3
  • 24
    • 0035869345 scopus 로고    scopus 로고
    • Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans
    • J.M. O'Sullivan, M.J. Mihr, M.A. Santos, and M.F. Tuite Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans Yeast 18 2001 313 322
    • (2001) Yeast , vol.18 , pp. 313-322
    • O'Sullivan, J.M.1    Mihr, M.J.2    Santos, M.A.3    Tuite, M.F.4
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology 276 1997 307 326
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0035951403 scopus 로고    scopus 로고
    • Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem
    • L. Ribas de Pouplana, and P. Schimmel Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem Cell 104 2001 191 193
    • (2001) Cell , vol.104 , pp. 191-193
    • Ribas De Pouplana, L.1    Schimmel, P.2
  • 27
    • 0027442959 scopus 로고
    • (Ser) domains to aminoacylation by E coli seryl-tRNA synthetase: A kinetic analysis using model RNA substrates
    • (Ser) domains to aminoacylation by E.coli seryl-tRNA synthetase: a kinetic analysis using model RNA substrates Nucleic Acids Res. 21 1993 4467 4475
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4467-4475
    • Sampson, J.R.1    Saks, M.E.2
  • 28
    • 0023061339 scopus 로고
    • Aminoacyl tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • P. Schimmel Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs Annu. Rev. Biochem. 56 1987 125 158
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 29
    • 0035788034 scopus 로고    scopus 로고
    • Formation of two classes of tRNA synthetases in relation to editing functions and genetic code
    • P. Schimmel, and L. Ribas de Pouplana Formation of two classes of tRNA synthetases in relation to editing functions and genetic code Cold Spring Harb. Symp. Quant. Biol. 66 2001 161 166
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 161-166
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 30
    • 0032190210 scopus 로고    scopus 로고
    • Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae
    • A. Soma, and H. Himeno Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae Nucleic Acids Res. 26 1998 4374 4381
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4374-4381
    • Soma, A.1    Himeno, H.2
  • 31
    • 0027741164 scopus 로고
    • (Ser) function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner
    • (Ser) function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner Nucleic Acids Res. 21 1993 5589 5594
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5589-5594
    • Wu, X.Q.1    Gross, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.