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Volumn 4, Issue 10, 1996, Pages 1141-1151

Helix unwinding in the effector region of elongation factor EF-Tu-GDP

Author keywords

conformational changes; effector region; elongation factor Tu; protein biosynthesis

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; THERMUS AQUATICUS;

EID: 0030587857     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00122-0     Document Type: Article
Times cited : (212)

References (37)
  • 1
    • 0003110793 scopus 로고
    • Factors involved in the transfer of aminoacyl-tRNA to the ribosome
    • Weisbach, H. & Petska, S., eds, Academic press, NY, USA
    • Miller, D.L. & Weisbach, H. (1977). Factors involved in the transfer of aminoacyl-tRNA to the ribosome. In Molecular Mechanism of Protein Biosynthesis. (Weisbach, H. & Petska, S., eds), pp. 323-373, Academic press, NY, USA.
    • (1977) Molecular Mechanism of Protein Biosynthesis , pp. 323-373
    • Miller, D.L.1    Weisbach, H.2
  • 2
    • 0023195033 scopus 로고
    • Effects of the mutation glycine-222· aspartic acid on the function of elongation factor Tu
    • Swart, G.W.M. & Parmeggiani, A. (1987). Effects of the mutation glycine-222· aspartic acid on the function of elongation factor Tu. Biochemistry 26, 2047-2054.
    • (1987) Biochemistry , vol.26 , pp. 2047-2054
    • Swart, G.W.M.1    Parmeggiani, A.2
  • 3
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield, J.J. (1974). Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. USA 71, 4135-4139.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 4
    • 0016793283 scopus 로고
    • Kinetic amplification of enzyme discrimination
    • Ninio, J. (1975). Kinetic amplification of enzyme discrimination. Biochimie 57, 587-595.
    • (1975) Biochimie , vol.57 , pp. 587-595
    • Ninio, J.1
  • 5
    • 0004955452 scopus 로고
    • Proofreading of the codon-anticodon interaction on ribosomes
    • Thompson, R.C. & Stone, P.J. (1977). Proofreading of the codon-anticodon interaction on ribosomes. Proc. Natl. Acad. Sci. USA 74, 198-202.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 198-202
    • Thompson, R.C.1    Stone, P.J.2
  • 6
    • 0020337390 scopus 로고
    • Is there proofreading during polypeptide synthesis?
    • Ruusala, T., Ehrenberg, M. & Kurland, C.G. (1982). Is there proofreading during polypeptide synthesis? EMBO J. 1, 741-745.
    • (1982) EMBO J. , vol.1 , pp. 741-745
    • Ruusala, T.1    Ehrenberg, M.2    Kurland, C.G.3
  • 7
    • 0014879045 scopus 로고
    • Studies on the purification and properties of factor Tu from E. coli
    • Miller, D.L. & Weissbach, H. (1970). Studies on the purification and properties of factor Tu from E. coli. Arch. Biochem. Biophys. 141, 26-37.
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 26-37
    • Miller, D.L.1    Weissbach, H.2
  • 8
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H.R., Sanders, D.A. & McCormick, F. (1990). The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 9
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, DA. & 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
  • 10
    • 0026588965 scopus 로고
    • Refined structure of elongation factor Tu from Escherichia coli
    • Kjeldgaard, M. & Nyborg, J. (1992). Refined structure of elongation factor 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
  • 11
    • 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
  • 13
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of Phe-tRNA Phe, EF-Tu, and a GTP analog
    • Nissen, P., et al., & Nyborg, J. (1995). Crystal structure of the ternary complex of Phe-tRNA Phe, EF-Tu, and a GTP analog. Science 270, 1464-1472.
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1    Nyborg, J.2
  • 14
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. & Leberman, R. (1996). The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution. Nature 379, 511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 15
    • 0020479686 scopus 로고
    • The elongation factor Tu binds aminoacyl-tRNA in the presence of GDP
    • Pingoud, A., Block, W., Wittinghofer, A., Wolf, H. & Fischer, E. (1982). The elongation factor Tu binds aminoacyl-tRNA in the presence of GDP. J. Biol. Chem. 257, 11261-11267.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11261-11267
    • Pingoud, A.1    Block, W.2    Wittinghofer, A.3    Wolf, H.4    Fischer, E.5
  • 16
    • 0017236878 scopus 로고
    • Limited hydrolysis of the polypeptide chain elongation factor Tu by trypsin
    • Arai, K., Nakamura, S., Arai, T., Kawakita, M. & Kaziro, Y. (1976). Limited hydrolysis of the polypeptide chain elongation factor Tu by trypsin. J. Biochem. 79, 69-83.
    • (1976) J. Biochem. , vol.79 , pp. 69-83
    • Arai, K.1    Nakamura, S.2    Arai, T.3    Kawakita, M.4    Kaziro, Y.5
  • 17
    • 0019034773 scopus 로고
    • Composition and properties of trypsin-cleaved elongation factor Tu
    • Wittinghoffer, A., Frank, R. & Leberman, R. (1989). Composition and properties of trypsin-cleaved elongation factor Tu. Eur. J. Biochem. 108, 423-431.
    • (1989) Eur. J. Biochem. , vol.108 , pp. 423-431
    • Wittinghoffer, A.1    Frank, R.2    Leberman, R.3
  • 18
    • 0017109833 scopus 로고
    • Crystals of partially trypsin-digested elongation factor Tu
    • Gast, W.H., Leberman, R., Schulz, G.E. & Wittinghofer, A. (1976). Crystals of partially trypsin-digested elongation factor Tu. J. Mol. Biol. 106, 943-950.
    • (1976) J. Mol. Biol. , vol.106 , pp. 943-950
    • Gast, W.H.1    Leberman, R.2    Schulz, G.E.3    Wittinghofer, A.4
  • 19
    • 0019740103 scopus 로고
    • Properties of native and nicked elongation factor Tu from Thermus thermophilus HB8
    • Gulewicz, K., Faulhammer, H.G. & Sprinzl, M. (1981). Properties of native and nicked elongation factor Tu from Thermus thermophilus HB8. Eur. J. Biochem. 121, 155-162.
    • (1981) Eur. J. Biochem. , vol.121 , pp. 155-162
    • Gulewicz, K.1    Faulhammer, H.G.2    Sprinzl, M.3
  • 20
    • 0025908019 scopus 로고
    • Characterization of a limited trypsin digestion form of eukaryotic elongation factor 1 a
    • Kinzy, T.G. & Merrick, W.C. (1991). Characterization of a limited trypsin digestion form of eukaryotic elongation factor 1 a. J. Biol. Chem. 266, 4099-4105.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4099-4105
    • Kinzy, T.G.1    Merrick, W.C.2
  • 21
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor, J.C., Harrison, D.H., Kahn, R.A. & Ringe, D. (1994). Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704-708.
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 22
    • 0029113233 scopus 로고
    • The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
    • Greasley, S.E., et al., & Bax, B. (1995). The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nat. Struct. Biol. 2, 797-806.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 797-806
    • Greasley, S.E.1    Bax, B.2
  • 23
    • 0028929866 scopus 로고
    • Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form
    • Scheffzek, K., Klebe, C., Fritz-Wolf, K., Kabsch, W. & Wittinghofer, A. (1995). Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374, 378-381.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 24
    • 0030584663 scopus 로고    scopus 로고
    • A complex profile of protein elongation: Translating chemical energy into molecular movement
    • 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
  • 25
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador, W.E., Means, A.R. & Quiocho, F.A. (1992). Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 26
    • 0024294054 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus
    • Lippmann, C., Betzel, C., Dauter, Z., Wilson, K. & Erdmann, V.A. (1988). Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus. FEBS Lett. 240, 139-140.
    • (1988) FEBS Lett. , vol.240 , pp. 139-140
    • Lippmann, C.1    Betzel, C.2    Dauter, Z.3    Wilson, K.4    Erdmann, V.A.5
  • 28
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds, Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, Daresbury Laboratory, Warrington, UK.
    • (1993) CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project No.4. (1994). The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 31
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 32
    • 0014432781 scopus 로고
    • Solvent content in protein crystals
    • Matthews, B.W. (1968). Solvent content in protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 33
    • 84967852329 scopus 로고
    • MERLOT: An integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald, P.M.D. (1988). MERLOT: an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Cryst. 21, 273-278.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 34
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for refinement of macromolecules
    • Tronrud, D.E. (1992). Conjugate-direction minimization: an improved method for refinement of macromolecules. Acta Cryst. A 48, 912-916.
    • (1992) Acta Cryst. A , vol.48 , pp. 912-916
    • Tronrud, D.E.1
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., 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. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Cowan, S.2    Zou, J.-Y.3    Kjeldgaard, M.4
  • 36
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A.T., Karplus, M. & Petsko, G.A. (1989). Crystallographic refinement by simulated annealing: application to crambin. Acta Cryst. A 45, 50-61.
    • (1989) Acta Cryst. A , vol.45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 37
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.