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Volumn 7, Issue 12, 1999, Pages 1575-1583

The Escherichia coli large ribosomal subunit at 7.5 Å resolution

Author keywords

50S ribosomal subunit; Angular reconstitution; Cryo electron microscopy; Ribosomal proteins; Ribosome structure

Indexed keywords

PROTEIN SUBUNIT; RIBOSOME PROTEIN;

EID: 0033573131     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)88348-3     Document Type: Article
Times cited : (117)

References (39)
  • 1
    • 0024007766 scopus 로고
    • Cryo-electron microscopy of vitrified specimens
    • 1. Dubochet, J., et al., & Schultz, P. (1988). Cryo-electron microscopy of vitrified specimens. Quart. Rev. Biophys. 21, 129-228.
    • (1988) Quart. Rev. Biophys. , vol.21 , pp. 129-228
    • Dubochet, J.1    Schultz, P.2
  • 2
    • 0029645318 scopus 로고
    • The 70S Escherichia coli ribosome at 23 Å resolution: Fitting the ribosomal RNA
    • 2. Stark, H., et al., & Van Heel, M. (1995). The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA. Structure 3, 815-821.
    • (1995) Structure , vol.3 , pp. 815-821
    • Stark, H.1    Van Heel, M.2
  • 3
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • 3. Van Heel, M. (1987). Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy 21, 111-124.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-124
    • Van Heel, M.1
  • 4
    • 0029100747 scopus 로고
    • A model of protein synthesis based on cryo-electron microscopy of the E. Coli ribosome
    • 4. Frank, J., et al., & Agrawal, R.K. (1995). A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376, 441-444.
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1    Agrawal, R.K.2
  • 5
    • 0030887834 scopus 로고    scopus 로고
    • Arrangement of the tRNAs in pre-and post-translocational ribosomes revealed by electron cryomicroscopy
    • 5. Stark, H., et al., & Van Heel, M. (1997). Arrangement of the tRNAs in pre-and post-translocational ribosomes revealed by electron cryomicroscopy. Cell 88, 19-28.
    • (1997) Cell , vol.88 , pp. 19-28
    • Stark, H.1    Van Heel, M.2
  • 7
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of the elongation factor G on E. coli 70S ribosome: The mechanism of translation
    • 7. Agrawal, K.R., Penczek, P., Grassucci, R.A. & Frank, J. (1998). Visualization of the elongation factor G on E. coli 70S ribosome: the mechanism of translation. Proc. Natl Acad. Sci. 95, 6134-6138.
    • (1998) Proc. Natl Acad. Sci. , vol.95 , pp. 6134-6138
    • Agrawal, K.R.1    Penczek, P.2    Grassucci, R.A.3    Frank, J.4
  • 9
    • 0004290179 scopus 로고    scopus 로고
    • A 9 Å resolution X-ray crystallographic map of the large ribosomal subunit
    • 9. Ban, N., et al., & Steitz, T.A. (1998). A 9 Å resolution X-ray crystallographic map of the large ribosomal subunit. Cell 93, 1105-1115.
    • (1998) Cell , vol.93 , pp. 1105-1115
    • Ban, N.1    Steitz, T.A.2
  • 10
    • 0033566668 scopus 로고    scopus 로고
    • Elucidating the structure of ribosomal particles: An interplay between electron-cryo-microscopy and X-ray crystallography
    • 10. Harms, J., et al., & Yonath, A. (1999). Elucidating the structure of ribosomal particles: an interplay between electron-cryo-microscopy and X-ray crystallography. Structure 7, 931-941.
    • (1999) Structure , vol.7 , pp. 931-941
    • Harms, J.1    Yonath, A.2
  • 11
    • 0001912470 scopus 로고    scopus 로고
    • Three-dimensional organisation of the bacterial ribosome and its subunits: The transition from low-resolution models to high-resolution structures
    • (Garrett, R.A., Douthwaite, S.R., Liljas, A., Matheson, A.T., Moore, P.B. & Noller, F.F., eds), ASM Press, Washington DC, in press
    • 11. Brimacombe, R., Greuer, B., Mueller, F., Osswald, M., Rinke-Appel, J., & Sommer, I. (1999). Three-dimensional organisation of the bacterial ribosome and its subunits: the transition from low-resolution models to high-resolution structures. In The Ribosome; Structure, Function, Antibiotics, and Cellular Interactions. (Garrett, R.A., Douthwaite, S.R., Liljas, A., Matheson, A.T., Moore, P.B. & Noller, F.F., eds), ASM Press, Washington DC, in press.
    • (1999) The Ribosome; Structure, Function, Antibiotics, and Cellular Interactions
    • Brimacombe, R.1    Greuer, B.2    Mueller, F.3    Osswald, M.4    Rinke-Appel, J.5    Sommer, I.6
  • 12
    • 0000665417 scopus 로고    scopus 로고
    • The structure of ribosomal RNA
    • 12. Brimacombe, R. (1999). The structure of ribosomal RNA. ASM Newsletters, 6, 144-151.
    • (1999) ASM Newsletters , vol.6 , pp. 144-151
    • Brimacombe, R.1
  • 13
    • 0033534198 scopus 로고    scopus 로고
    • Nucleotides in 23S rRNA protected by the association of 30S and 50S ribosomal subunits
    • 13. Merryman, C., Moazed, D., Daubresse, G. & Noller, H.F. (1999). Nucleotides in 23S rRNA protected by the association of 30S and 50S ribosomal subunits. J. Mol. Biol. 285, 107-113.
    • (1999) J. Mol. Biol. , vol.285 , pp. 107-113
    • Merryman, C.1    Moazed, D.2    Daubresse, G.3    Noller, H.F.4
  • 14
    • 0030937751 scopus 로고    scopus 로고
    • Visualisation of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • 14. Conway, J., Cheng, N., Wingfield, P.T., Stahl, S.J. & Steven, A.C. (1997). Visualisation of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 385, 91-94.
    • (1997) Nature , vol.385 , pp. 91-94
    • Conway, J.1    Cheng, N.2    Wingfield, P.T.3    Stahl, S.J.4    Steven, A.C.5
  • 15
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • 15. Böttcher, B., Wynne, S.A. & Crowther, R.A. (1997). Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386, 88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 17
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution
    • 17. Orlova, E.V., et al., & Van Heel, M. (1997). Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution, J. Mol. Biol. 271, 417-437.
    • (1997) J. Mol. Biol. , vol.271 , pp. 417-437
    • Orlova, E.V.1    Van Heel, M.2
  • 18
    • 0030596154 scopus 로고    scopus 로고
    • Ribosomal protein L9: A structure determination by the combined use of X-ray crystallography and NMR spectroscopy
    • 18. Hoffman, D.W., Cameron, C.S., Davies, C., White, S. & Ramakrishnan, V. (1996). Ribosomal protein L9: a structure determination by the combined use of X-ray crystallography and NMR spectroscopy. J. Mol. Biol. 264, 1058-1071.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1058-1071
    • Hoffman, D.W.1    Cameron, C.S.2    Davies, C.3    White, S.4    Ramakrishnan, V.5
  • 19
    • 0039425732 scopus 로고
    • Location of eight ribosomal proteins on the surface of the 50S subunit from Escherichia coli
    • 19. Stöffler-Meilicke, M., Noah, M., & Stöffler, G. (1983). Location of eight ribosomal proteins on the surface of the 50S subunit from Escherichia coli. Proc. Natl Acad. Sci. USA 80, 6780-6784.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 6780-6784
    • Stöffler-Meilicke, M.1    Noah, M.2    Stöffler, G.3
  • 20
    • 0031214378 scopus 로고    scopus 로고
    • An exceptionally stable helix from the ribosomal protein L9: Implications for protein folding and stability
    • 20. Kuhlman, B., Yang, H.Y., Boice, J.A., Fairman, R. & Raleigh, D.P. (1997). An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability. J. Mol. Biol. 270, 640-647.
    • (1997) J. Mol. Biol. , vol.270 , pp. 640-647
    • Kuhlman, B.1    Yang, H.Y.2    Boice, J.A.3    Fairman, R.4    Raleigh, D.P.5
  • 21
    • 0029444686 scopus 로고
    • The ribosomal environment of tRNA:Cross-links to rRNA from positions 8 and 20:1 in the central fold of tRNA located at the A, P or E site
    • 21. Rinke-Appel, J., Jünke, N., Osswald, M. & Brimacombe, R. (1995). The ribosomal environment of tRNA:cross-links to rRNA from positions 8 and 20:1 in the central fold of tRNA located at the A, P or E site. RNA 1, 1018-1028.
    • (1995) RNA , vol.1 , pp. 1018-1028
    • Rinke-Appel, J.1    Jünke, N.2    Osswald, M.3    Brimacombe, R.4
  • 22
    • 0033151862 scopus 로고    scopus 로고
    • The environment of 5S rRNA in the ribosome: Cross-links to 23S rRNA from sites within helices II and III of the 5S molecule
    • 22. Osswald, M. & Brimacombe, R. (1999). The environment of 5S rRNA in the ribosome: cross-links to 23S rRNA from sites within helices II and III of the 5S molecule. Nucleic Acids Res. 27, 2283-2290.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2283-2290
    • Osswald, M.1    Brimacombe, R.2
  • 23
    • 0030801742 scopus 로고    scopus 로고
    • A new model for the three-dimensional folding of Escherichia coli 16S ribosomal RNA. I. Fitting the RNA to a 3D electron microscopic map at 20 Å
    • 23. Mueller, F. & Brimacombe, R. (1997). A new model for the three-dimensional folding of Escherichia coli 16S ribosomal RNA. I. Fitting the RNA to a 3D electron microscopic map at 20 Å. J. Mol. Biol. 271, 524-544.
    • (1997) J. Mol. Biol. , vol.271 , pp. 524-544
    • Mueller, F.1    Brimacombe, R.2
  • 24
    • 0030821676 scopus 로고    scopus 로고
    • A new model for the three-dimensional folding of Escherichia coli 16S ribosomal RNA. II. The RNA-protein interaction data
    • 24. Mueller, F. & Brimacombe, R. (1997). A new model for the three-dimensional folding of Escherichia coli 16S ribosomal RNA. II. The RNA-protein interaction data. J. Mol. Biol. 271, 545-565.
    • (1997) J. Mol. Biol. , vol.271 , pp. 545-565
    • Mueller, F.1    Brimacombe, R.2
  • 25
    • 0032521188 scopus 로고    scopus 로고
    • The 80S rat liver ribosome at 25 Å resolution by electron microscopy and angular reconstruction
    • 25. Dube, P., et al., & Van Heel, M. (1998). The 80S rat liver ribosome at 25 Å resolution by electron microscopy and angular reconstruction. Structure 6, 398-399.
    • (1998) Structure , vol.6 , pp. 398-399
    • Dube, P.1    Van Heel, M.2
  • 26
    • 0029402859 scopus 로고
    • Location and domain structure of Escherichia coli ribosomal protein L7/L12: Site specific cysteine crosslinking and attachment of fluorescent probes
    • 26. Traut, R.R., et al., & Jameson, D. (1995). Location and domain structure of Escherichia coli ribosomal protein L7/L12: site specific cysteine crosslinking and attachment of fluorescent probes. Biochem. Cell Biol. 73, 949-958.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 949-958
    • Traut, R.R.1    Jameson, D.2
  • 27
    • 0001115404 scopus 로고
    • On the structure, function, and dynamics of L7/L12 from Escherichia coli ribosomes
    • (Hardesty, B. & Kramer, G., eds), Springer-Verlag, Berlin
    • 27. Möller, W. & Maassen, J.A. (1986). On the structure, function, and dynamics of L7/L12 from Escherichia coli ribosomes. In Structure, Function, and Genetics of Ribosomes. (Hardesty, B. & Kramer, G., eds), Springer-Verlag, Berlin.
    • (1986) Structure, Function, and Genetics of Ribosomes
    • Möller, W.1    Maassen, J.A.2
  • 28
    • 0025807709 scopus 로고
    • The binding site of ribosomal protein L10 in eubacteria and archaebacteria is conserved: Reconstitution of chimeric 50S subunits
    • 28. Stöffler-Meilicke, M. & Stöffler, G. (1991). The binding site of ribosomal protein L10 in eubacteria and archaebacteria is conserved: reconstitution of chimeric 50S subunits. Biochimie 73, 797-804.
    • (1991) Biochimie , vol.73 , pp. 797-804
    • Stöffler-Meilicke, M.1    Stöffler, G.2
  • 29
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5 Å resolution map of the 50S ribosomal subunit
    • 29. Ban, N., Nissen, P., Hansen, J., Capel, M., Moore, P.B. & Steitz, T.A. (1999). Placement of protein and RNA structures into a 5 Å resolution map of the 50S ribosomal subunit. Nature 400, 841-847.
    • (1999) Nature , vol.400 , pp. 841-847
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Capel, M.4    Moore, P.B.5    Steitz, T.A.6
  • 31
    • 0032849011 scopus 로고    scopus 로고
    • Identification of an RNA-protein bridge spanning the ribosomal subunit interface
    • 31. Culver, G.M., Cate, J.H., Yusupova, G.Z., Yusupov, M.M. & Noller, H.F. (1999). Identification of an RNA-protein bridge spanning the ribosomal subunit interface. Science 285, 2133-2136.
    • (1999) Science , vol.285 , pp. 2133-2136
    • Culver, G.M.1    Cate, J.H.2    Yusupova, G.Z.3    Yusupov, M.M.4    Noller, H.F.5
  • 32
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structures of 70S ribosome functional complexes
    • 32. Cate, J.H., Yusupov, M.M., Yusupova, G.Z., Earnest, T.N. & Noller, H.F. (1999). X-ray crystal structures of 70S ribosome functional complexes. Science 285, 2095-2104.
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 34
    • 0001312477 scopus 로고
    • Classification of very large electron microscopical image data sets
    • 34. Van Heel, M. (1989). Classification of very large electron microscopical image data sets. Optik 82, 114-126.
    • (1989) Optik , vol.82 , pp. 114-126
    • Van Heel, M.1
  • 35
    • 0000313739 scopus 로고
    • Exact filters for general geometry three-dimensional reconstruction
    • 35. Harauz, G. & Van Heel, M. (1986). Exact filters for general geometry three-dimensional reconstruction. Optik 73, 146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    Van Heel, M.2
  • 36
    • 0020484054 scopus 로고
    • Comparison of 4 x 6-meric hemocyanins from three different arthropods using computer alignment and correspondence analysis
    • 36. Bijlholt, M.M.C., Van Heel, M.G. & Van Bruggen, E.F.J. (1982). Comparison of 4 x 6-meric hemocyanins from three different arthropods using computer alignment and correspondence analysis. J. Mol. Biol. 161, 139-153.
    • (1982) J. Mol. Biol. , vol.161 , pp. 139-153
    • Bijlholt, M.M.C.1    Van Heel, M.G.2    Van Bruggen, E.F.J.3
  • 37
    • 0026564434 scopus 로고
    • Magnification mismatches between micrographs: Corrective procedures and implications for structural analysis
    • 37. Aldroubi, A., Trus, B.L., Unser, M., Booy, F.P. & Steven, A.C. (1992). Magnification mismatches between micrographs: corrective procedures and implications for structural analysis. Ultramicroscopy 46, 175-188.
    • (1992) Ultramicroscopy , vol.46 , pp. 175-188
    • Aldroubi, A.1    Trus, B.L.2    Unser, M.3    Booy, F.P.4    Steven, A.C.5
  • 38
    • 0030933355 scopus 로고    scopus 로고
    • Template convolution to enhance or detect structural features in macromolecualr electron-density maps
    • 38. Kleywegt, G.J. & Jones, T.A. (1997). Template convolution to enhance or detect structural features in macromolecualr electron-density maps. Acta Crystallogr. D 53, 179-185.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 179-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • 39. Jones, T.A. & Kjeldgaard, M. (1997). Electron-density map interpretation. Methods Enzymol. 277 B, 173-207.
    • (1997) Methods Enzymol. , vol.277 B , pp. 173-207
    • Jones, T.A.1    Kjeldgaard, M.2


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