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Volumn 370, Issue 1, 2007, Pages 128-141

Structural Insights into the Second Step of RNA-dependent Cysteine Biosynthesis in Archaea: Crystal Structure of Sep-tRNA:Cys-tRNA Synthase from Archaeoglobus fulgidus

Author keywords

crystal structure; cysteine; phosphoserine; PLP; tRNA

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL RNA; CYSTEINE; CYSTEINE TRANSFER RNA; DIMER; MONOMER; PYRIDOXAL 5 PHOSPHATE;

EID: 34249337418     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.050     Document Type: Article
Times cited : (36)

References (22)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M., and Soll D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69 (2000) 617-650
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 2
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273 (1996) 1058-1073
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5    Sutton, G.G.6
  • 4
    • 34247234997 scopus 로고    scopus 로고
    • Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea
    • Fukunaga R., and Yokoyama S. Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Nature Struct. Mol. Biol. 14 (2007) 272-279
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 272-279
    • Fukunaga, R.1    Yokoyama, S.2
  • 6
    • 0036303444 scopus 로고    scopus 로고
    • Analysis of the E. coli NifS CsdB protein at 2.0 Å reveals the structural basis for perselenide and persulfide intermediate formation
    • Lima C.D. Analysis of the E. coli NifS CsdB protein at 2.0 Å reveals the structural basis for perselenide and persulfide intermediate formation. J. Mol. Biol. 315 (2002) 1199-1208
    • (2002) J. Mol. Biol. , vol.315 , pp. 1199-1208
    • Lima, C.D.1
  • 7
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly
    • Kaiser J.T., Clausen T., Bourenkow G.P., Bartunik H.D., Steinbacher S., and Huber R. Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. J. Mol. Biol. 297 (2000) 451-464
    • (2000) J. Mol. Biol. , vol.297 , pp. 451-464
    • Kaiser, J.T.1    Clausen, T.2    Bourenkow, G.P.3    Bartunik, H.D.4    Steinbacher, S.5    Huber, R.6
  • 8
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: their function and mechanisms
    • Mihara H., and Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Biotechnol. 60 (2002) 12-23
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 9
    • 0034673177 scopus 로고    scopus 로고
    • Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase
    • Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., and Hata Y. Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry 39 (2000) 1263-1273
    • (2000) Biochemistry , vol.39 , pp. 1263-1273
    • Fujii, T.1    Maeda, M.2    Mihara, H.3    Kurihara, T.4    Esaki, N.5    Hata, Y.6
  • 10
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 12
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng L., White R.H., Cash V.L., Jack R.F., and Dean D.R. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl Acad. Sci. USA 90 (1993) 2754-2758
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 13
    • 0032553428 scopus 로고    scopus 로고
    • The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate
    • Lacourciere G.M., and Stadtman T.C. The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. J. Biol. Chem. 273 (1998) 30921-30926
    • (1998) J. Biol. Chem. , vol.273 , pp. 30921-30926
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 14
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies
    • Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., and Esaki N. A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies. J. Biol. Chem. 274 (1999) 14768-14772
    • (1999) J. Biol. Chem. , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 16
    • 33845763611 scopus 로고    scopus 로고
    • RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
    • Yuan J., Palioura S., Salazar J.C., Su D., O'Donoghue P., Hohn M.J., et al. RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc. Natl Acad. Sci. USA 103 (2006) 18923-18927
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18923-18927
    • Yuan, J.1    Palioura, S.2    Salazar, J.C.3    Su, D.4    O'Donoghue, P.5    Hohn, M.J.6
  • 17
    • 33745587780 scopus 로고    scopus 로고
    • Structural basis of RNA-dependent recruitment of glutamine to the genetic code
    • Oshikane H., Sheppard K., Fukai S., Nakamura Y., Ishitani R., Numata T., et al. Structural basis of RNA-dependent recruitment of glutamine to the genetic code. Science 312 (2006) 1950-1954
    • (2006) Science , vol.312 , pp. 1950-1954
    • Oshikane, H.1    Sheppard, K.2    Fukai, S.3    Nakamura, Y.4    Ishitani, R.5    Numata, T.6
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
    • CCP41
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the streochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the streochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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