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Volumn 53, Issue 12, 2014, Pages 1916-1924

Structural basis of improved second-generation 3-nitro-tyrosine tRNA synthetases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PROTEINS;

EID: 84898062419     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5001239     Document Type: Article
Times cited : (49)

References (32)
  • 2
    • 84857451064 scopus 로고    scopus 로고
    • Designer proteins: Applications of genetic code expansion in cell biology
    • Davis, L. and Chin, J. W. (2012) Designer proteins: applications of genetic code expansion in cell biology Nat. Rev. Mol. Cell. Biol. 13, 168-182
    • (2012) Nat. Rev. Mol. Cell. Biol. , vol.13 , pp. 168-182
    • Davis, L.1    Chin, J.W.2
  • 4
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C. C. and Schultz, P. G. (2010) Adding new chemistries to the genetic code Annu. Rev. Biochem. 79, 413-444
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 5
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L., Brock, A., Herberich, B., and Schultz, P. G. (2001) Expanding the genetic code of Escherichia coli Science 292, 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 7
    • 67650354415 scopus 로고    scopus 로고
    • Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins
    • Abello, N., Kerstjens, H. A., Postma, D. S., and Bischoff, R. (2009) Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins J. Proteome. Res. 8, 3222-3238
    • (2009) J. Proteome. Res. , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.2    Postma, D.S.3    Bischoff, R.4
  • 8
    • 4444258355 scopus 로고    scopus 로고
    • Proteomic method for identification of tyrosine-nitrated proteins
    • Aulak, K. S., Koeck, T., Crabb, J. W., and Stuehr, D. J. (2004) Proteomic method for identification of tyrosine-nitrated proteins Methods Mol. Biol. 279, 151-165
    • (2004) Methods Mol. Biol. , vol.279 , pp. 151-165
    • Aulak, K.S.1    Koeck, T.2    Crabb, J.W.3    Stuehr, D.J.4
  • 9
    • 84877738843 scopus 로고    scopus 로고
    • Bioinformatics analysis reveals biophysical and evolutionary insights into the 3-nitrotyrosine post-translational modification in the human proteome
    • Ng, J. Y., Boelen, L., and Wong, J. W. (2013) Bioinformatics analysis reveals biophysical and evolutionary insights into the 3-nitrotyrosine post-translational modification in the human proteome Open Biol. 3, 120148
    • (2013) Open Biol. , vol.3 , pp. 120148
    • Ng, J.Y.1    Boelen, L.2    Wong, J.W.3
  • 12
    • 84863173015 scopus 로고    scopus 로고
    • A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum
    • Wang, Y. S., Fang, X., Wallace, A. L., Wu, B., and Liu, W. R. (2012) A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum J. Am. Chem. Soc. 134, 2950-2953
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2950-2953
    • Wang, Y.S.1    Fang, X.2    Wallace, A.L.3    Wu, B.4    Liu, W.R.5
  • 14
    • 51649087417 scopus 로고    scopus 로고
    • Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog
    • Oki, K., Sakamoto, K., Kobayashi, T., Sasaki, H. M., and Yokoyama, S. (2008) Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog Proc. Natl. Acad. Sci. U.S.A. 105, 13298-13303
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13298-13303
    • Oki, K.1    Sakamoto, K.2    Kobayashi, T.3    Sasaki, H.M.4    Yokoyama, S.5
  • 15
    • 77954380484 scopus 로고    scopus 로고
    • Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion
    • Iraha, F., Oki, K., Kobayashi, T., Ohno, S., Yokogawa, T., Nishikawa, K., Yokoyama, S., and Sakamoto, K. (2010) Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion Nucleic Acids Res. 38, 3682-3691
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3682-3691
    • Iraha, F.1    Oki, K.2    Kobayashi, T.3    Ohno, S.4    Yokogawa, T.5    Nishikawa, K.6    Yokoyama, S.7    Sakamoto, K.8
  • 17
    • 84867583216 scopus 로고    scopus 로고
    • Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion
    • Heinemann, I. U., Rovner, A. J., Aerni, H. R., Rogulina, S., Cheng, L., Olds, W., Fischer, J. T., Soll, D., Isaacs, F. J., and Rinehart, J. (2012) Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion FEBS Lett. 586, 3716-3722
    • (2012) FEBS Lett. , vol.586 , pp. 3716-3722
    • Heinemann, I.U.1    Rovner, A.J.2    Aerni, H.R.3    Rogulina, S.4    Cheng, L.5    Olds, W.6    Fischer, J.T.7    Soll, D.8    Isaacs, F.J.9    Rinehart, J.10
  • 19
    • 0030757720 scopus 로고    scopus 로고
    • TNT refinement package
    • Tronrud, D. E. (1997) TNT refinement package Methods Enzymol. 277, 306-319
    • (1997) Methods Enzymol. , vol.277 , pp. 306-319
    • Tronrud, D.E.1
  • 20
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics Acta Crystallogr., D 60, 2126-2132
    • (2004) Acta Crystallogr., D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 22
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr. D 62, 439-450
    • (2006) Acta Crystallogr. D , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 24
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman, K. L. and Pease, L. R. (2007) Gene splicing and mutagenesis by PCR-driven overlap extension Nat. Protoc. 2, 924-932
    • (2007) Nat. Protoc. , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 26
    • 23644445334 scopus 로고    scopus 로고
    • Photo-cross-linking interacting proteins with a genetically encoded benzophenone
    • Farrell, I. S., Toroney, R., Hazen, J. L., Mehl, R. A., and Chin, J. W. (2005) Photo-cross-linking interacting proteins with a genetically encoded benzophenone Nat. Methods 2, 377-384
    • (2005) Nat. Methods , vol.2 , pp. 377-384
    • Farrell, I.S.1    Toroney, R.2    Hazen, J.L.3    Mehl, R.A.4    Chin, J.W.5
  • 28
    • 68949117722 scopus 로고    scopus 로고
    • Enhancing the utility of unnatural amino acid synthetases by manipulating broad substrate specificity
    • Stokes, A. L., Miyake-Stoner, S. J., Peeler, J. C., Nguyen, D. P., Hammer, R. P., and Mehl, R. A. (2009) Enhancing the utility of unnatural amino acid synthetases by manipulating broad substrate specificity Mol. Biosyst. 5, 1032-1038
    • (2009) Mol. Biosyst. , vol.5 , pp. 1032-1038
    • Stokes, A.L.1    Miyake-Stoner, S.J.2    Peeler, J.C.3    Nguyen, D.P.4    Hammer, R.P.5    Mehl, R.A.6
  • 29
    • 17744373680 scopus 로고    scopus 로고
    • Crystal structures of apo wild-type M jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for o-methyl-L-tyrosine
    • Zhang, Y., Wang, L., Schultz, P. G., and Wilson, I. A. (2005) Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for o-methyl-L-tyrosine Protein Sci. 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
  • 30
    • 27544505167 scopus 로고    scopus 로고
    • Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase
    • Turner, J. M., Graziano, J., Spraggon, G., and Schultz, P. G. (2005) Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase J. Am. Chem. Soc. 127, 14976-14977
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14976-14977
    • Turner, J.M.1    Graziano, J.2    Spraggon, G.3    Schultz, P.G.4
  • 31
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs, K. and Karplus, P. A. (1997) Improved R-factors for diffraction data analysis in macromolecular crystallography Nat. Struct. Biol. 4, 269-275
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 32
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A. and Diederichs, K. (2012) Linking crystallographic model and data quality Science 336, 1030-1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.