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Volumn 78, Issue 11-12, 1996, Pages 921-933

The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold

Author keywords

Aminoacyl tRNA; EF Tu; GTP; Recognition; Ternary complex

Indexed keywords

AMINO ACID; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE DERIVATIVE; SELENOCYSTEINE; SYNTHETASE; TRANSFER RNA;

EID: 0030433926     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)86714-4     Document Type: Conference Paper
Times cited : (53)

References (62)
  • 1
    • 0003110793 scopus 로고
    • Factors involved in the transfer of aminoacyl-tRNA to the ribosome
    • (Weissbach H, Petska S, eds) Academic Press, New York
    • 1 Miller DL, Weissbach H (1977) Factors Involved in the transfer of aminoacyl-tRNA to the ribosome. In: Molecular Mechanisms of Protein Biosynthesis (Weissbach H, Petska S, eds) Academic Press, New York, 323-373
    • (1977) Molecular Mechanisms of Protein Biosynthesis , pp. 323-373
    • Miller, D.L.1    Weissbach, H.2
  • 2
    • 0018089806 scopus 로고
    • The role of guanosine 5-triphosphate in polypeptide elongation
    • 2 Kaziro Y (1978) The role of guanosine 5-triphosphate in polypeptide elongation. Biochem Biophys Acta 505, 95-127
    • (1978) Biochem Biophys Acta , vol.505 , pp. 95-127
    • Kaziro, Y.1
  • 4
    • 0030584663 scopus 로고    scopus 로고
    • A complex profile of protein elongation: Translating chemical energy into molecular movement
    • 4 Abel K, Jurnak F ( 1996) A complex profile of protein elongation: translating chemical energy into molecular movement. Structure 4, 229-238
    • (1996) Structure , vol.4 , pp. 229-238
    • Abel, K.1    Jurnak, F.2
  • 5
    • 0030091227 scopus 로고    scopus 로고
    • Imprinting through molecular mimicry
    • 5 Liljas A (1996) Imprinting through molecular mimicry. Curr Biol 6, 247-249
    • (1996) Curr Biol , vol.6 , pp. 247-249
    • Liljas, A.1
  • 6
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • in press
    • 6 Nakamura Y, Ito K, Isaksson L (1996) Emerging understanding of translation termination. Cell, in press
    • (1996) Cell
    • Nakamura, Y.1    Ito, K.2    Isaksson, L.3
  • 8
    • 0023190457 scopus 로고
    • Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu
    • 8 Faulhammer HG, Joshi RL (1987) Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu. FEBS Lett 217, 203-211
    • (1987) FEBS Lett , vol.217 , pp. 203-211
    • Faulhammer, H.G.1    Joshi, R.L.2
  • 9
    • 0000528185 scopus 로고
    • Recognition of aminoacyl-tRNAs by protein elongation factors
    • (Söll S, RajBhandary U, eds) American Society for Microbiology, Washington, DC
    • 9 Clark BFC, Kjeldgaard M, Barciszewski J, Sprinzl M (1994) Recognition of aminoacyl-tRNAs by protein elongation factors. In: tRNA: Structure, Biosynthesis and Function (Söll S, RajBhandary U, eds) American Society for Microbiology, Washington, DC, 423-442
    • (1994) TRNA: Structure, Biosynthesis and Function , pp. 423-442
    • Clark, B.F.C.1    Kjeldgaard, M.2    Barciszewski, J.3    Sprinzl, M.4
  • 10
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 10 Jones TA, Cowan S, Zou J-Y, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A46, 110-119
    • (1991) Acta Cryst , vol.A46 , pp. 110-119
    • Jones, T.A.1    Cowan, S.2    Zou, J.-Y.3    Kjeldgaard, M.4
  • 11
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • 11 Engh RA, Huber R (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst A47, 392-400
    • (1991) Acta Cryst , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 11644328584 scopus 로고
    • Systematic analysis of structural data as a research technique in organic chemistry
    • 13 Allen FH, Kennard O, Taylor R (1983) Systematic analysis of structural data as a research technique in organic chemistry. Acc Chem Res 16, 146-153
    • (1983) Acc Chem Res , vol.16 , pp. 146-153
    • Allen, F.H.1    Kennard, O.2    Taylor, R.3
  • 14
    • 0025348355 scopus 로고
    • How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
    • 14 Ehrenberg M, Rojas AM, Weiser J, Kurland CG (1990) How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation? J Mol Biol 211, 739-749
    • (1990) J Mol Biol , vol.211 , pp. 739-749
    • Ehrenberg, M.1    Rojas, A.M.2    Weiser, J.3    Kurland, C.G.4
  • 15
    • 0028304633 scopus 로고
    • Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?
    • 15 Weijland A, Parmeggiani A (1994) Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis? Trends Biochem Sci 19, 188-193
    • (1994) Trends Biochem Sci , vol.19 , pp. 188-193
    • Weijland, A.1    Parmeggiani, A.2
  • 16
    • 0028848882 scopus 로고
    • Two GTPs are consumed on EF-Tu per peptide bond in poly (Phe) synthesis, in spite of switching stoichiometry of the EF-Tu aminoacyl-tRNA complex with temperature
    • 16 Dincbas V, Bilgin N, Scoble J, Ehrenberg M (1995) Two GTPs are consumed on EF-Tu per peptide bond in poly (Phe) synthesis, in spite of switching stoichiometry of the EF-Tu aminoacyl-tRNA complex with temperature. FEBS Lett 357, 19-22
    • (1995) FEBS Lett , vol.357 , pp. 19-22
    • Dincbas, V.1    Bilgin, N.2    Scoble, J.3    Ehrenberg, M.4
  • 17
    • 0028241947 scopus 로고
    • Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu
    • 17 Rüdinger J, Blechschmidt B, Ribeiro S, Sprinzl M (1994) Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu. Biochemistry 33, 5682-5688
    • (1994) Biochemistry , vol.33 , pp. 5682-5688
    • Rüdinger, J.1    Blechschmidt, B.2    Ribeiro, S.3    Sprinzl, M.4
  • 18
    • 0023261832 scopus 로고
    • Differences between transfer RNA molecules
    • 18 Mcclain WH, Nicholas HB (1987) Differences between transfer RNA molecules. J Mol Biol 194, 635-642
    • (1987) J Mol Biol , vol.194 , pp. 635-642
    • McClain, W.H.1    Nicholas, H.B.2
  • 19
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • 19 Rould MA, Perona JJ, Steitz TA (1991) Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352, 213-219
    • (1991) Nature , vol.352 , pp. 213-219
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 21
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T thermophilus seryl-tRNA synthetase complexed with tRNA (Ser)
    • 21 Biou V, Yaremchuk A, Tukalo M, Cusack S (1994) The 2.9 Å crystal structure of T thermophilus seryl-tRNA synthetase complexed with tRNA (Ser). Science 263, 1404-1410
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 22
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • 22 Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 23
    • 0023710643 scopus 로고
    • Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor
    • 23 Motorin Yu A, Wolfson AD, Orlovsky AF, Gladilin KL (1988) Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. FEBS Lett 238, 262-264
    • (1988) FEBS Lett , vol.238 , pp. 262-264
    • Motorin Yu, A.1    Wolfson, A.D.2    Orlovsky, A.F.3    Gladilin, K.L.4
  • 24
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • 24 Kjeldgaard M, Nissen P, Thirup S, Nyborg J (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1, 35-50
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 25
    • 0029151201 scopus 로고
    • CH-p interactions in the packing of the adenine ring in protein structures
    • 25 Chakrabarti P, Samanta U (1995) CH-p interactions in the packing of the adenine ring in protein structures. J Mol Biol 251, 9-14
    • (1995) J Mol Biol , vol.251 , pp. 9-14
    • Chakrabarti, P.1    Samanta, U.2
  • 27
    • 0019872620 scopus 로고
    • Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu
    • 27 Duffy LK, Gerber L, Johnson AE, Miller DL (1981) Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu. Biochemistry 20, 4663-4666
    • (1981) Biochemistry , vol.20 , pp. 4663-4666
    • Duffy, L.K.1    Gerber, L.2    Johnson, A.E.3    Miller, D.L.4
  • 28
    • 0028219577 scopus 로고
    • Effector region of the translation elongation factor EF-Tu.GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex
    • 28 Förster C, Limmer S, Zeidler W, Sprinzl M (1994) Effector region of the translation elongation factor EF-Tu.GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex. Proc Natl Acad Sci USA 91, 4254-4257
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4254-4257
    • Förster, C.1    Limmer, S.2    Zeidler, W.3    Sprinzl, M.4
  • 29
    • 0022412615 scopus 로고
    • Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5′-triphosphate-aminoacyl-tRNA complexes
    • 29 Louie A, Jurnak F (1985) Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5′-triphosphate-aminoacyl-tRNA complexes. Biochemistry 24, 6433-6439
    • (1985) Biochemistry , vol.24 , pp. 6433-6439
    • Louie, A.1    Jurnak, F.2
  • 30
    • 0029548957 scopus 로고
    • Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: Effects on the GTPase reaction and aminoacyl-tRNA binding
    • 30 Knudsen CR, Clark BFC (1995) Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: effects on the GTPase reaction and aminoacyl-tRNA binding. Prot Eng 8, 1267-1273
    • (1995) Prot Eng , vol.8 , pp. 1267-1273
    • Knudsen, C.R.1    Clark, B.F.C.2
  • 31
    • 0025019432 scopus 로고
    • The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy
    • 31 Ott G, Jonak J, Abrahams IP, Sprinzl M (1990) The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy. Nucleic Acids Res 18, 437-441
    • (1990) Nucleic Acids Res , vol.18 , pp. 437-441
    • Ott, G.1    Jonak, J.2    Abrahams, I.P.3    Sprinzl, M.4
  • 32
    • 0028895690 scopus 로고
    • Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots
    • 32 Kjærsgard IV, Knudsen CR, Wiborg O (1995) Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots. Eur J Biochem 228, 184-190
    • (1995) Eur J Biochem , vol.228 , pp. 184-190
    • Kjærsgard, I.V.1    Knudsen, C.R.2    Wiborg, O.3
  • 33
    • 0029786512 scopus 로고    scopus 로고
    • Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA
    • 33 Wiborg O, Andersen C, Knudsen CR, Clark BFC, Nyborg J (1996) Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. J Biol Chem 271, 20406-20411
    • (1996) J Biol Chem , vol.271 , pp. 20406-20411
    • Wiborg, O.1    Andersen, C.2    Knudsen, C.R.3    Clark, B.F.C.4    Nyborg, J.5
  • 34
    • 0029094248 scopus 로고
    • Recruiting proteins to the RNA world
    • 34 Mattaj IW, Nagai K (1995) Recruiting proteins to the RNA world. Nature Struct Biol 2, 518-522
    • (1995) Nature Struct Biol , vol.2 , pp. 518-522
    • Mattaj, I.W.1    Nagai, K.2
  • 35
    • 0026556564 scopus 로고
    • A model for the aminoacyl-tRNA binding site of eukaryotic elongation factor 1 alpha
    • 35 Kinzy TG, Freeman JP, Johnson AE, Merrick WC (1992) A model for the aminoacyl-tRNA binding site of eukaryotic elongation factor 1 alpha. J Biol Chem 267, 1623-1632
    • (1992) J Biol Chem , vol.267 , pp. 1623-1632
    • Kinzy, T.G.1    Freeman, J.P.2    Johnson, A.E.3    Merrick, W.C.4
  • 36
    • 0016361235 scopus 로고
    • Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu
    • 36 Wolf H, Chinali G, Parmeggiani A (1974) Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu. Proc Natl Acad Sci 71, 4910-4914
    • (1974) Proc Natl Acad Sci , vol.71 , pp. 4910-4914
    • Wolf, H.1    Chinali, G.2    Parmeggiani, A.3
  • 37
    • 0028000039 scopus 로고
    • The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in E coli
    • 37 Mesters JR, Zeef LA, Hilgenfeld R, Graaf JMd, Kraal B, Bosch L (1994) The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in E coli. EMBO J 1354, 4877-4885
    • (1994) EMBO J , vol.1354 , pp. 4877-4885
    • Mesters, J.R.1    Zeef, L.A.2    Hilgenfeld, R.3    Graaf, J.Md.4    Kraal, B.5    Bosch, L.6
  • 38
    • 0028018013 scopus 로고
    • Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu:GTP
    • 38 Abdulkarim F, Liljas L, Hughes D (1995) Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu:GTP. FEBS Lett 352, 118-122
    • (1995) FEBS Lett , vol.352 , pp. 118-122
    • Abdulkarim, F.1    Liljas, L.2    Hughes, D.3
  • 39
    • 0029990096 scopus 로고    scopus 로고
    • Mutants of EF-Tu defective in binding aminoacyl-tRNA
    • 39 Abdulkarim F, Ehrenberg M, Hughes D (1996) Mutants of EF-Tu defective in binding aminoacyl-tRNA. FEBS Lett 382, 297-303
    • (1996) FEBS Lett , vol.382 , pp. 297-303
    • Abdulkarim, F.1    Ehrenberg, M.2    Hughes, D.3
  • 40
    • 0028214276 scopus 로고
    • Fusidic acid-resistant mutants define three regions in elongation factor G of salmonella typhimurium
    • 40 Johanson U, Hughes D (1994) Fusidic acid-resistant mutants define three regions in elongation factor G of salmonella typhimurium. Gene 143, 55-59
    • (1994) Gene , vol.143 , pp. 55-59
    • Johanson, U.1    Hughes, D.2
  • 46
    • 0016394367 scopus 로고
    • Nuclear magnetic resonance studies of protein-RNA interactions. I. The elongation factor Tu-GTP aminoacyl-tRNA complex
    • 46 Schulman RG, Hilbers CW, Miller DL (1974) Nuclear magnetic resonance studies of protein-RNA interactions. I. The elongation factor Tu-GTP aminoacyl-tRNA complex. J Mol Biol 90, 601-607
    • (1974) J Mol Biol , vol.90 , pp. 601-607
    • Schulman, R.G.1    Hilbers, C.W.2    Miller, D.L.3
  • 47
    • 0027994489 scopus 로고
    • Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP
    • 47 Barciszewski J, Sprinzl M, Clark BF (1994) Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP. FEBS Lett 351, 137-139
    • (1994) FEBS Lett , vol.351 , pp. 137-139
    • Barciszewski, J.1    Sprinzl, M.2    Clark, B.F.3
  • 48
    • 0025280236 scopus 로고
    • Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: Evidence for a new functional role for elongation factor Tu in protein biosynthesis
    • 48 Janiak F, Dell VA, Abrahamson JK, Watson BS, Miller DL, Johnson AE (1990) Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Biochemistry 29, 4268-4277
    • (1990) Biochemistry , vol.29 , pp. 4268-4277
    • Janiak, F.1    Dell, V.A.2    Abrahamson, J.K.3    Watson, B.S.4    Miller, D.L.5    Johnson, A.E.6
  • 49
    • 0029767729 scopus 로고    scopus 로고
    • Evidence for aminoacylation-induced conformational changes in human mitochondrial tRNAs
    • 49 Enriquez JA, Attardi G (1996) Evidence for aminoacylation-induced conformational changes in human mitochondrial tRNAs. Proc Natl Acad Sci USA 93, 8300-8305
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8300-8305
    • Enriquez, J.A.1    Attardi, G.2
  • 50
    • 0007388960 scopus 로고
    • The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins
    • 50 Lee CP, Mandal N, Dyson MR, RajBhandary UL (1993) The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins. Proc Natl Acad Sci USA 90, 7149-7152
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7149-7152
    • Lee, C.P.1    Mandal, N.2    Dyson, M.R.3    RajBhandary, U.L.4
  • 51
    • 0020017428 scopus 로고
    • Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: Effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure
    • 51 Tanada S, Kawakami M, Nishio K, Takemura S (1982) Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure. J Biochem Tokyo 91, 291-299
    • (1982) J Biochem Tokyo , vol.91 , pp. 291-299
    • Tanada, S.1    Kawakami, M.2    Nishio, K.3    Takemura, S.4
  • 52
    • 0025103403 scopus 로고
    • Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E coll
    • 52 Förster C, Ott G, Forchhammer K, Sprinzl M (1990) Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E coll. Nucleic Acids Res 18, 487-491
    • (1990) Nucleic Acids Res , vol.18 , pp. 487-491
    • Förster, C.1    Ott, G.2    Forchhammer, K.3    Sprinzl, M.4
  • 53
    • 0013914711 scopus 로고
    • The role of N-formyl-methionine-sRNA in protein synthesis
    • 53 Clark BFC, Marcker KA (1966) The role of N-formyl-methionine-sRNA in protein synthesis. J Mol Biol 17, 394-406
    • (1966) J Mol Biol , vol.17 , pp. 394-406
    • Clark, B.F.C.1    Marcker, K.A.2
  • 54
    • 0029563262 scopus 로고
    • Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation
    • 54 Ævarsson A (1995) Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation. J Mol Evol 41, 1096-1104
    • (1995) J Mol Evol , vol.41 , pp. 1096-1104
    • ÆVarsson, A.1
  • 55
    • 0024988324 scopus 로고
    • The role of modified purine 64 in initiator/elongator discrimination of tRNA (iMet) from yeast and wheat germ
    • 55 Kiesewetter S, Ott G, Sprinzl M (1990) The role of modified purine 64 in initiator/elongator discrimination of tRNA (iMet) from yeast and wheat germ. Nucleic Acids Res 18, 4677-4682
    • (1990) Nucleic Acids Res , vol.18 , pp. 4677-4682
    • Kiesewetter, S.1    Ott, G.2    Sprinzl, M.3
  • 56
    • 0027745663 scopus 로고
    • Discrimination between initiation and elongation of protein biosynthesis in yeast: Identity assured by a nucleotide modification in the initiator tRNA
    • 56 Förster C, Chakraburtty K, Sprinzl M (1993) Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA. Nucleic Acids Res 21, 5679-5683
    • (1993) Nucleic Acids Res , vol.21 , pp. 5679-5683
    • Förster, C.1    Chakraburtty, K.2    Sprinzl, M.3
  • 57
    • 0028034499 scopus 로고
    • Ritl, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination
    • 57 Åström SU, Byström AS (1994) Ritl, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination. Cell 79, 535-546
    • (1994) Cell , vol.79 , pp. 535-546
    • Åström, S.U.1    Byström, A.S.2
  • 58
    • 0024420343 scopus 로고
    • Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein
    • 58 Forchhammer K, Leinfelder W, Bock A (1989) Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature 342, 453-456
    • (1989) Nature , vol.342 , pp. 453-456
    • Forchhammer, K.1    Leinfelder, W.2    Bock, A.3
  • 60
    • 0030568977 scopus 로고    scopus 로고
    • Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB
    • 60 Kromayer M, Wilting R, Tormay P, Böck A (1996) Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. J Mol Biol 262, 413-420
    • (1996) J Mol Biol , vol.262 , pp. 413-420
    • Kromayer, M.1    Wilting, R.2    Tormay, P.3    Böck, A.4
  • 62
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 62 Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24, 946-950
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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