메뉴 건너뛰기




Volumn 4, Issue 5, 1996, Pages 555-565

The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange

Author keywords

Antibiotic resistance; Conformational transitions; Elongation factor G; GTPases; Protein synthesis

Indexed keywords

ELONGATION FACTOR; ELONGATION FACTOR G; GUANOSINE DIPHOSPHATE; MAGNESIUM;

EID: 0030585061     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00061-5     Document Type: Article
Times cited : (130)

References (43)
  • 1
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A. & McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0001941152 scopus 로고
    • Some structural aspects of elongation
    • Hill, W.E., Dahlberg, A., Garrett, R.A., Moore, P.B., Schlessinger, D. & Warner, J.R., eds, American Society of Microbiology, Washington DC
    • Liljas, A. (1990). Some structural aspects of elongation. In The ribosome: structure, function & evolution. (Hill, W.E., Dahlberg, A., Garrett, R.A., Moore, P.B., Schlessinger, D. & Warner, J.R., eds), pp. 309-317, American Society of Microbiology, Washington DC.
    • (1990) The Ribosome: Structure, Function & Evolution , pp. 309-317
    • Liljas, A.1
  • 3
    • 0022319403 scopus 로고
    • Ribosomal translocation: Facts and models
    • Spirin, A.S. (1985). Ribosomal translocation: facts and models. Prog. Nucleic Acids Res. Mol. Biol. 32, 75-114.
    • (1985) Prog. Nucleic Acids Res. Mol. Biol. , vol.32 , pp. 75-114
    • Spirin, A.S.1
  • 4
    • 0018089806 scopus 로고
    • The role of guanosine 5′-triphosphate in polypeptide chain elongation
    • Kaziro, Y. (1978). The role of guanosine 5′-triphosphate in polypeptide chain elongation. Biochim. Biophys. Acta 505, 95-127.
    • (1978) Biochim. Biophys. Acta , vol.505 , pp. 95-127
    • Kaziro, Y.1
  • 5
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 angstrom resolution
    • Czworkowski, J., Wang, J., Steitz, T.A. & Moore, P.B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 angstrom resolution. EMBO J. 13, 3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 6
    • 0028059544 scopus 로고
    • Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus
    • Ævarsson, A., et al., & Liljas, A. (1994). Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13, 3669-3677.
    • (1994) EMBO J. , vol.13 , pp. 3669-3677
    • ÆVarsson, A.1    Liljas, A.2
  • 7
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J. & Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 9
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus Aquaticus in the GTP conformation
    • 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
  • 10
    • 0027132717 scopus 로고
    • The 2.2 A crystal structure of transducin-α complexed with GTPγS
    • Noel, J.P., Hamm, H.E. & Sigler, P.B. (1993). The 2.2 A crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-662.
    • (1993) Nature , vol.366 , pp. 654-662
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 11
    • 0029563262 scopus 로고
    • Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation
    • 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
  • 12
    • 0029182369 scopus 로고
    • A ribosomal protein module in EF-G and DNA gyrase
    • Murzin, A.G. (1995). A ribosomal protein module in EF-G and DNA gyrase. Nat. Struct. Biol. 2, 25-26.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 25-26
    • Murzin, A.G.1
  • 13
    • 0026687213 scopus 로고
    • The structure of ribosomal protein-S5 reveals sites of interaction with 16S rRNA
    • Ramakrishnan, V. & White, S.W. (1992). The structure of ribosomal protein-S5 reveals sites of interaction with 16S rRNA. Nature 358, 768-771.
    • (1992) Nature , vol.358 , pp. 768-771
    • Ramakrishnan, V.1    White, S.W.2
  • 14
    • 0028203301 scopus 로고
    • Crystal structure of the ribosomal protein S6 from Thermus thermophilus
    • Lindahl, M., et al., & Amons, R. (1994). Crystal structure of the ribosomal protein S6 from Thermus thermophilus. EMBO J. 13, 1249-1254.
    • (1994) EMBO J. , vol.13 , pp. 1249-1254
    • Lindahl, M.1    Amons, R.2
  • 15
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T.H., Li, J. & Evans, P.R. (1990). Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 348, 515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 16
    • 0030025671 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution: Mechanism of GDP/GTP exchange
    • Kawashima, T., Berthet-Colominas, C., Cusack, S., Wulff, M. & Leberman, R. (1996). The crystal structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution: mechanism of GDP/GTP exchange. Nature 379, 511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Cusack, S.3    Wulff, M.4    Leberman, R.5
  • 17
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of the PhetRNA, elongation factor Tu and a GTP analogue
    • Nissen, P., et al., & Nyborg, J. (1995). Crystal structure of the ternary complex of the PhetRNA, elongation factor Tu and a GTP analogue. Science 270, 1464-1472.
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1    Nyborg, J.2
  • 18
    • 0020437699 scopus 로고
    • Structural studies of ribosomes
    • Liljas, A. (1982). Structural studies of ribosomes. Prog. Biophys. Mol. Biol. 40, 161-228.
    • (1982) Prog. Biophys. Mol. Biol. , vol.40 , pp. 161-228
    • Liljas, A.1
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical feature
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical feature. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0023692465 scopus 로고
    • The switch between two conformations of adenylate kinase
    • Dreusicke, D. & Schultz, G.E. (1988). The switch between two conformations of adenylate kinase. J. Mol. Biol. 203, 1021-1028.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1021-1028
    • Dreusicke, D.1    Schultz, G.E.2
  • 21
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G.W., Lutter, R. & Walker, J.E. (1994). Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 23
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn, M.V., et al., & Kim, S.-H. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Kim, S.-H.2
  • 24
    • 0026588965 scopus 로고
    • Refined structure of elongation factor-EF-Tu from Escherichia coli
    • Kjeldgaard, M. & Nyborg, J. (1992). Refined structure of elongation factor-EF-Tu from Escherichia coli. J. Mol. Biol. 223, 721-742.
    • (1992) J. Mol. Biol. , vol.223 , pp. 721-742
    • Kjeldgaard, M.1    Nyborg, J.2
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J,-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 147, 110-119.
    • (1991) Acta Crystallogr. A , vol.147 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0028237708 scopus 로고
    • Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
    • Lambright, D.G., Noel, J.P., Hamm, H.E. & Sigler, P.B. (1994). Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Nature 369, 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 28
    • 0025094188 scopus 로고
    • Novel mutants of elongation factor G
    • Richter Dalfors, A. & Kurland, C.G. (1990). Novel mutants of elongation factor G. J. Mol. Biol. 215, 549-557.
    • (1990) J. Mol. Biol. , vol.215 , pp. 549-557
    • Richter Dalfors, A.1    Kurland, C.G.2
  • 29
    • 0028214276 scopus 로고
    • Fusidic acid-resistant mutants define three regions in elongation factor G of Salmonella typhimurium
    • 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
  • 30
    • 0028018013 scopus 로고
    • Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu-GTP
    • Abdulkarim, F., Liljas, L. & Hughes, D. (1994). Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu-GTP FEBS Lett. 352, 118-122.
    • (1994) FEBS Lett. , vol.352 , pp. 118-122
    • Abdulkarim, F.1    Liljas, L.2    Hughes, D.3
  • 31
    • 0029002506 scopus 로고
    • Phosphorylation of elongation factor Tu prevents ternary complex formation
    • Alexander, C., et al., & Lippmann, C. (1995). Phosphorylation of elongation factor Tu prevents ternary complex formation. J. Biol. Chem. 270, 14541-14547.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14541-14547
    • Alexander, C.1    Lippmann, C.2
  • 32
    • 0014636203 scopus 로고
    • A model of the functioning ribosome: Locking and unlocking of the ribosome subparticles
    • Spirin, A.S. (1969). A model of the functioning ribosome: locking and unlocking of the ribosome subparticles. Cold Spring Harbor Symp. Quant. Biol. 34, 197-207.
    • (1969) Cold Spring Harbor Symp. Quant. Biol. , vol.34 , pp. 197-207
    • Spirin, A.S.1
  • 33
    • 0002676922 scopus 로고
    • The ribosomal components involved in EF-G and EF-Tu- dependent GTP hydrolysis
    • Nomura, M., Tissiéres, A., & Lengyel, P., eds, Cold Spring Harbor Laboratory, NY
    • Möller, W. (1974) . The ribosomal components involved in EF-G and EF-Tu- dependent GTP hydrolysis. In Ribosomes. (Nomura, M., Tissiéres, A., & Lengyel, P., eds), pp. 711-731, Cold Spring Harbor Laboratory, NY.
    • (1974) Ribosomes , pp. 711-731
    • Möller, W.1
  • 34
    • 0028135617 scopus 로고
    • Synergism between the GTPase activities of EF-Tu·GTP and EF-G·GTP on empty ribosomes - Elongation factors as stimulators of the ribosomal oscillation between two conformations
    • Mesters, J.R., Potapov, A.P., Degraaf, J.M. & Kraal, B. (1994). Synergism between the GTPase activities of EF-Tu·GTP and EF-G·GTP on empty ribosomes - elongation factors as stimulators of the ribosomal oscillation between two conformations. J. Mol. Biol. 242, 644-654.
    • (1994) J. Mol. Biol. , vol.242 , pp. 644-654
    • Mesters, J.R.1    Potapov, A.P.2    Degraaf, J.M.3    Kraal, B.4
  • 35
    • 10644269258 scopus 로고
    • Crystallization of elongation factor G from an extreme thermophile, Thermus thermophilus HB8
    • Reshetnikova, L.S. & Garber, M.B. (1983). Crystallization of elongation factor G from an extreme thermophile, Thermus thermophilus HB8. FEBS Lett. 154, 149-150.
    • (1983) FEBS Lett. , vol.154 , pp. 149-150
    • Reshetnikova, L.S.1    Garber, M.B.2
  • 36
    • 0030565976 scopus 로고    scopus 로고
    • Crystallization and structural studies of components of the protein synthesizing system from Thermus thermophilus
    • in press
    • Garber, M., et al., & Al-Karadaghi S., (1996). Crystallization and structural studies of components of the protein synthesizing system from Thermus thermophilus. J. Cryst. Growth, in press.
    • (1996) J. Cryst. Growth
    • Garber, M.1    Al-Karadaghi, S.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 39
    • 84945096204 scopus 로고
    • Model bias in macromoleculer structures
    • Hodel, A., Kim, S.-H. & Brunger, A.T. (1992). Model bias in macromoleculer structures. Acta Cryst. A 48, 851-858.
    • (1992) Acta Cryst. A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brunger, A.T.3
  • 40
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure coordinates
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structure coordinates. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 41
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 43
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A.C., Laskowski, R.A. & Thornton, J.M. (1995). LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 143-146.
    • (1995) Protein Eng. , vol.8 , pp. 143-146
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.