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Volumn 18, Issue 6, 1999, Pages 1459-1467

The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome

Author keywords

Peptidyl transferase; Ribosomal protein L2; RNA binding protein; X ray structure

Indexed keywords

PEPTIDYLTRANSFERASE; RIBOSOME PROTEIN; RNA 23S; RNA BINDING PROTEIN;

EID: 0033559924     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.6.1459     Document Type: Article
Times cited : (58)

References (59)
  • 1
    • 0030847766 scopus 로고    scopus 로고
    • Protein data bank archives of three-dimensional macromolecular structures
    • Abola, E.E., Sussman, J.L., Prilusky, J. and Manning, N.O. (1997) Protein data bank archives of three-dimensional macromolecular structures. Methods Enzymol., 276, 556-571.
    • (1997) Methods Enzymol. , vol.276 , pp. 556-571
    • Abola, E.E.1    Sussman, J.L.2    Prilusky, J.3    Manning, N.O.4
  • 2
    • 0030855279 scopus 로고    scopus 로고
    • Bias reduction in phase refinement by modified interference functions: Introducing the gamma correction
    • Abrahams, J.-P. (1997) Bias reduction in phase refinement by modified interference functions: introducing the gamma correction. Acta Crystallogr., D53, 371-376.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 371-376
    • Abrahams, J.-P.1
  • 4
    • 0024116796 scopus 로고
    • The binding site for ribosomal protein L2 within 23S ribosomal RNA of Escherichia coli
    • Beauclerk, A.A. and Cundliffe, E. (1988) The binding site for ribosomal protein L2 within 23S ribosomal RNA of Escherichia coli. EMBO J., 7, 3589-3594.
    • (1988) EMBO J. , vol.7 , pp. 3589-3594
    • Beauclerk, A.A.1    Cundliffe, E.2
  • 5
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., Pfuetzner, R.A., Edwards, A.M. and Frappier, L. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature, 385, 176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 6
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 7
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., D54, 905-921.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Brünger, A.T.1
  • 8
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft, M., Hubbard, T.J., Proctor, M., Freund, S.M. and Murzin, A.G. (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.2    Proctor, M.3    Freund, S.M.4    Murzin, A.G.5
  • 9
    • 0023572210 scopus 로고
    • A complete mapping of the proteins in the small ribosomal subunit of Escherichia coli
    • Capel, M.S. et al. (1987) A complete mapping of the proteins in the small ribosomal subunit of Escherichia coli. Science, 238, 1403-1406.
    • (1987) Science , vol.238 , pp. 1403-1406
    • Capel, M.S.1
  • 10
    • 0027411514 scopus 로고
    • Yeast tRNA (Asp) recognition by its cognate class II aminoacyl-tRNA synthetase
    • Cavarelli, J., Rees, B., Ruff, M., Thierry, J.C. and Morask, D. (1993) Yeast tRNA (Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature, 362, 181-184.
    • (1993) Nature , vol.362 , pp. 181-184
    • Cavarelli, J.1    Rees, B.2    Ruff, M.3    Thierry, J.C.4    Morask, D.5
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 12
    • 0029402170 scopus 로고
    • Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity
    • Cooperman, B.S., Wooten, T., Romero, D.P. and Traut, R.R. (1995) Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity. Biochem. Cell. Biol. 73, 1087-1094.
    • (1995) Biochem. Cell. Biol. , vol.73 , pp. 1087-1094
    • Cooperman, B.S.1    Wooten, T.2    Romero, D.P.3    Traut, R.R.4
  • 13
    • 84983681648 scopus 로고
    • A nitrogen gas stream cryostat for general x-ray diffraction studies
    • Cosier, J. and Glazer, A.M. (1986) A nitrogen gas stream cryostat for general X-ray diffraction studies. J. Appl. Crystallogr., 19, 105-107.
    • (1986) J. Appl. Crystallogr. , vol.19 , pp. 105-107
    • Cosier, J.1    Glazer, A.M.2
  • 14
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • de la Fortelle, E. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Fortelle, E.1    Bricogne, G.2
  • 15
    • 0026409151 scopus 로고
    • Attachment sites of primary binding proteins L1, L2 and L23 on 23S ribosomal RNA of Escherichia coli
    • Egebjerg, J., Christiansen, J. and Garrett, R.A. (1991) Attachment sites of primary binding proteins L1, L2 and L23 on 23S ribosomal RNA of Escherichia coli. J. Mol. Biol., 222, 251-264.
    • (1991) J. Mol. Biol. , vol.222 , pp. 251-264
    • Egebjerg, J.1    Christiansen, J.2    Garrett, R.A.3
  • 16
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr., D47, 392-400.
    • (1991) Acta Crystallogr. , vol.D47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 17
    • 0016816807 scopus 로고
    • Evidence of the involvement of a 50S ribosomal protein in several active sites
    • Fahnestock, S.R. (1975) Evidence of the involvement of a 50S ribosomal protein in several active sites. Biochemistry. 14, 5321-5327.
    • (1975) Biochemistry , vol.14 , pp. 5321-5327
    • Fahnestock, S.R.1
  • 18
    • 0015926832 scopus 로고
    • Reconstitution of 50S ribosomal subunits from protein-free ribonucleic acid
    • Fahnestock, S., Erdmann, V. and Nomura, M. (1973) Reconstitution of 50S ribosomal subunits from protein-free ribonucleic acid. Biochemistry, 12, 220-224.
    • (1973) Biochemistry , vol.12 , pp. 220-224
    • Fahnestock, S.1    Erdmann, V.2    Nomura, M.3
  • 20
    • 0021239982 scopus 로고
    • High resolution localization of the tRNA anticodon interaction site on the Escherichia coli 30S ribosomal subunit
    • Gornicki, P., Nurse, K., Hellmann, W., Boublik, M. and Ofengand, J. (1984) High resolution localization of the tRNA anticodon interaction site on the Escherichia coli 30S ribosomal subunit. J. Biol. Chem., 259, 10493-10498.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10493-10498
    • Gornicki, P.1    Nurse, K.2    Hellmann, W.3    Boublik, M.4    Ofengand, J.5
  • 21
    • 0024284020 scopus 로고
    • RNA-protein cross-linking in escherichia coli 50S ribosomal subunits: Determination of sites on 23S RNA that are cross-linked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane
    • Guile, H., Hoppe, E., Osswald, M., Greuer, B., Brimacombe, R. and Stoffler, G. (1988) RNA-protein cross-linking in Escherichia coli 50S ribosomal subunits: determination of sites on 23S RNA that are cross-linked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane. Nucleic Acids Res., 16, 815-832.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 815-832
    • Guile, H.1    Hoppe, E.2    Osswald, M.3    Greuer, B.4    Brimacombe, R.5    Stoffler, G.6
  • 22
    • 0019508396 scopus 로고
    • Ribosomal components from Escherichia coli 50S subunits involved in the reconstitution of peptidyltransferase activity
    • Hample, H., Schulze, H. and Nierhaus, K.H. (1981) Ribosomal components from Escherichia coli 50S subunits involved in the reconstitution of peptidyltransferase activity. J. Biol. Chem., 256, 2284-2288.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2284-2288
    • Hample, H.1    Schulze, H.2    Nierhaus, K.H.3
  • 23
    • 0032421820 scopus 로고    scopus 로고
    • Identification by site-directed mutagenesis of amino acid residues in ribosomal protein L2 that are essential for binding to 23S ribosomal RNA
    • Harada, N., Maemura, K., Yamasaki, N. and Kimura, M. (1998) Identification by site-directed mutagenesis of amino acid residues in ribosomal protein L2 that are essential for binding to 23S ribosomal RNA. Biochim Biophys Acta, 1429, 176-186.
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 176-186
    • Harada, N.1    Maemura, K.2    Yamasaki, N.3    Kimura, M.4
  • 24
    • 0029896213 scopus 로고    scopus 로고
    • Site-directed hydroxyl radical probing of the rRNA neighborhood of ribosomal protein S5
    • Heilek, G.M. and Noller, H.F. (1996) Site-directed hydroxyl radical probing of the rRNA neighborhood of ribosomal protein S5. Science. 272, 1659-1662.
    • (1996) Science. , vol.272 , pp. 1659-1662
    • Heilek, G.M.1    Noller, H.F.2
  • 25
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0032167995 scopus 로고    scopus 로고
    • Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution
    • Kim, K.K., Hung, L.-W., Yokota, H., Kim.R. and Kim, S.-H. (1998) Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution. Proc. Natl Acad. Sci. USA, 95, 10419-10424.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10419-10424
    • Kim, K.K.1    Hung, L.-W.2    Yokota, H.3    Kim, S.-H.4
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol., 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 32
    • 0022063262 scopus 로고
    • A new type of x-ray area detector utilizing laser stimulated luminescience
    • Miyahara, J., Takahashi, K., Amemiya, Y., Kamiya, N. and Satow, Y. (1986) A new type of X-ray area detector utilizing laser stimulated luminescience. Nucl. Instrum. Methods, A246, 572-578.
    • (1986) Nucl. Instrum. Methods , vol.A246 , pp. 572-578
    • Miyahara, J.1    Takahashi, K.2    Amemiya, Y.3    Kamiya, N.4    Satow, Y.5
  • 33
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. (1993) OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 34
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 35
    • 0032419766 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray crystallographic study of 23S rRNA binding domain of the ribosomal protein L2 from Bacillus stearothermophilus
    • in press
    • Nakashima, T., Kimura, M., Nakagawa, A. and Tanaka, I. (1999) Crystallization and preliminary X-ray crystallographic study of 23S rRNA binding domain of the ribosomal protein L2 from Bacillus stearothermophilus. J. Struct. Biol., in press.
    • (1999) J. Struct. Biol.
    • Nakashima, T.1    Kimura, M.2    Nakagawa, A.3    Tanaka, I.4
  • 36
    • 0028800949 scopus 로고
    • A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
    • Narayana, N., Matthews, D.A., Howell, E.E. and Nguyen-huu, X. (1995) A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site. Nature Struct. Biol., 2, 1018-1025.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1018-1025
    • Narayana, N.1    Matthews, D.A.2    Howell, E.E.3    Nguyen-Huu, X.4
  • 37
    • 9144224578 scopus 로고
    • Analysis of the assembly and function of the 50S subunit from Escherichia coli ribosomes by reconstitution
    • Chambliss, G. (ed.). University Park Press, Baltimore, MD
    • Nierhaus, K.H. (1980) Analysis of the assembly and function of the 50S subunit from Escherichia coli ribosomes by reconstitution. In Chambliss, G. (ed.), Ribosomes. University Park Press, Baltimore, MD, pp. 267-297.
    • (1980) Ribosomes , pp. 267-297
    • Nierhaus, K.H.1
  • 39
    • 0032584644 scopus 로고    scopus 로고
    • Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domains
    • Nitta, I., Kamada, Y., Noda, H., Ueda, T. and Watanabe, K. (1998) Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domains. Science, 281, 666-669.
    • (1998) Science , vol.281 , pp. 666-669
    • Nitta, I.1    Kamada, Y.2    Noda, H.3    Ueda, T.4    Watanabe, K.5
  • 40
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller, H.F., Hoffarth, V. and Zimniak, L. (1992) Unusual resistance of peptidyl transferase to protein extraction procedures. Science, 256, 1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 A resolution of the RNA-bimling domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.H. and Nagai, K. (1994) Crystal structure at 1.92 A resolution of the RNA-bimling domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature, 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 43
    • 0032530708 scopus 로고    scopus 로고
    • Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution
    • Peat, T.S., Newman, J., Waldo, G.S., Berendzen, J. and Terwilliger, T.C. (1998) Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution. Structure, 6, 1207-1214.
    • (1998) Structure , vol.6 , pp. 1207-1214
    • Peat, T.S.1    Newman, J.2    Waldo, G.S.3    Berendzen, J.4    Terwilliger, T.C.5
  • 44
    • 0032102374 scopus 로고    scopus 로고
    • Ribosomal protein structures: Insights into the architecture, machinery and evolution of the ribosome
    • Ramakrishnan, V. and White, S.W. (1998) Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome. Trends Biochem. Sci., 23, 208-212.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 208-212
    • Ramakrishnan, V.1    White, S.W.2
  • 45
    • 0001455061 scopus 로고
    • Weissenberg camera for macromolecules with imaging plate data collection system at the photon factory: Present status and future plan
    • Sakabe, N., Ikemizu, S., Sakabe, K., Higashi, T., Nakagawa, A., Watanabe, N., Adachi, S. and Sasaki, K. (1995) Weissenberg camera for macromolecules with imaging plate data collection system at the Photon Factory: present status and future plan. Rev. Sci. Instrum., 66, 1276-1281.
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 1276-1281
    • Sakabe, N.1    Ikemizu, S.2    Sakabe, K.3    Higashi, T.4    Nakagawa, A.5    Watanabe, N.6    Adachi, S.7    Sasaki, K.8
  • 46
    • 0002088672 scopus 로고
    • Numerical tables of anomalous scattering factors calculated by the Cromer and Liberman's method
    • Sasaki, S. (1989) Numerical tables of anomalous scattering factors calculated by the Cromer and Liberman's method. KEK Report, 88-14, 1-136.
    • (1989) KEK Report , pp. 88-114
    • Sasaki, S.1
  • 47
    • 0021767069 scopus 로고
    • A ribosomal protein that is immunologically conserved in archaebacteria, eubacteria and eukaryotes
    • Schmid, G., Strobel, O., Stoffler-Meilicke, M., Stoffler, G. and Bock, A. (1984) A ribosomal protein that is immunologically conserved in archaebacteria, eubacteria and eukaryotes, FEBS Lett., 177, 189-194.
    • (1984) FEBS Lett. , vol.177 , pp. 189-194
    • Schmid, G.1    Strobel, O.2    Stoffler-Meilicke, M.3    Stoffler, G.4    Bock, A.5
  • 48
    • 0020341129 scopus 로고
    • Minimal set of ribosomal components for reconstitution of the peptidyl transferase activity
    • Schulze, H. and Nierhaus, K.H. (1982) Minimal set of ribosomal components for reconstitution of the peptidyl transferase activity. EMBO J., 1, 609-613.
    • (1982) EMBO J. , vol.1 , pp. 609-613
    • Schulze, H.1    Nierhaus, K.H.2
  • 49
    • 0031045587 scopus 로고    scopus 로고
    • Patterson superposition and ab initio phasing
    • Sheldrick, G. (1997) Patterson superposition and ab initio phasing. Methods Enzymol., 276, 628-641.
    • (1997) Methods Enzymol. , vol.276 , pp. 628-641
    • Sheldrick, G.1
  • 50
    • 0020671323 scopus 로고
    • Structure and functions of ribosomal protein S1
    • Subramanian, A.R. (1983) Structure and functions of ribosomal protein S1. Prog. Nucleic Acid Res. Mol. Biol., 28, 101-142.
    • (1983) Prog. Nucleic Acid Res. Mol. Biol. , vol.28 , pp. 101-142
    • Subramanian, A.R.1
  • 51
    • 0026090429 scopus 로고
    • Modification of histidine residues on proteins from the 50S subunit of the Escherichia coli ribosome. Effects on subunit assembly and peptidyl transferase centre activity
    • Sumpter, V.G., Tate, W.P., Nowotny, P. and Nierhaus, K.H. (1991) Modification of histidine residues on proteins from the 50S subunit of the Escherichia coli ribosome. Effects on subunit assembly and peptidyl transferase centre activity. Eur. J. Biochem., 196, 255-260.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 255-260
    • Sumpter, V.G.1    Tate, W.P.2    Nowotny, P.3    Nierhaus, K.H.4
  • 52
    • 0031979738 scopus 로고    scopus 로고
    • Matching the crystallographic structure of ribosomal protein S7 to a three-dimensional model of the 16S ribosomal RNA
    • Tanaka, I., Nakagawa, A., Hosaka, H., Wakatsuki, S., Mueller, F. and Brimacombe, R. (1998) Matching the crystallographic structure of ribosomal protein S7 to a three-dimensional model of the 16S ribosomal RNA. RNA, 4, 542-550.
    • (1998) RNA , vol.4 , pp. 542-550
    • Tanaka, I.1    Nakagawa, A.2    Hosaka, H.3    Wakatsuki, S.4    Mueller, F.5    Brimacombe, R.6
  • 53
    • 0000434996 scopus 로고
    • Mounting of crystals for macromolecular crystallography in a free-standing thin film
    • Teng, T. (1990) Mounting of crystals for macromolecular crystallography in a free-standing thin film. J. Appl. Crystallogr., 23, 387-391.
    • (1990) J. Appl. Crystallogr. , vol.23 , pp. 387-391
    • Teng, T.1
  • 54
    • 0022393402 scopus 로고
    • Location of the binding region for 23S ribosomal RNA on ribosomal protein L2 from Bacillus stearothermophilus
    • Watanabe, K. and Kimura, M. (1985) Location of the binding region for 23S ribosomal RNA on ribosomal protein L2 from Bacillus stearothermophilus. Eur. J. Biochem., 153, 299-304.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 299-304
    • Watanabe, K.1    Kimura, M.2
  • 55
    • 24844463082 scopus 로고
    • A new macromolecular crystallography station on the beamline Bl-18B at the photon factory
    • Watanabe, N., Adachi, S., Nakagawa, A. and Sakabe, N. (1993) A new macromolecular crystallography station on the beamline BL-18B at the Photon Factory. Acta Crystallogr., A49, 14.
    • (1993) Acta Crystallogr. , vol.A49 , pp. 14
    • Watanabe, N.1    Adachi, S.2    Nakagawa, A.3    Sakabe, N.4
  • 56
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains
    • Wilson, K.P., Shewchuk, L.M., Brennan, R.G., Otsuka, A.J. and Matthews, B.W. (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains. Proc. Natl Acad. Sci. USA, 89, 9257-9261.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 58
    • 0029643950 scopus 로고
    • Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk
    • Wu, X., Knudsen, B., Feller, S.M., Zheng, J., Sali, A., Cowburn, D., Hanafusa, H. and Kuriyan, J. (1995) Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure, 3, 215-226.
    • (1995) Structure , vol.3 , pp. 215-226
    • Wu, X.1    Knudsen, B.2    Feller, S.M.3    Zheng, J.4    Sali, A.5    Cowburn, D.6    Hanafusa, H.7    Kuriyan, J.8
  • 59
    • 0031026205 scopus 로고    scopus 로고
    • New RNA recognition features revealed in ancient ribosomal proteins
    • Yonath, A. and Franceschi, F. (1997) New RNA recognition features revealed in ancient ribosomal proteins. Nature Struct. Biol., 4. 3-5.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 3-5
    • Yonath, A.1    Franceschi, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.