메뉴 건너뛰기




Volumn 12, Issue 7, 2004, Pages 1165-1176

Joint X-ray and NMR refinement of the yeast L30e-mRNA complex

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; IMINO ACID; PROTON; RNA;

EID: 3142608984     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.04.023     Document Type: Article
Times cited : (57)

References (34)
  • 1
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 0028103275 scopus 로고
    • The (Collaborative Computational Project, Number 4) CCP4 suite: Programs for protein crystallography
    • CCP4 The (Collaborative Computational Project, Number 4) CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 4
    • 0037470556 scopus 로고    scopus 로고
    • Inherent protein structural flexibility at the RNA-binding interface of L30e
    • Chao J.A., Prasad G.S., White S.A., Stout C.D., Williamson J.R. Inherent protein structural flexibility at the RNA-binding interface of L30e. J. Mol. Biol. 326:2003;999-1004
    • (2003) J. Mol. Biol. , vol.326 , pp. 999-1004
    • Chao, J.A.1    Prasad, G.S.2    White, S.A.3    Stout, C.D.4    Williamson, J.R.5
  • 5
    • 0027021650 scopus 로고
    • NMR and X-ray analysis of the three-dimensional structure of interleukin-8
    • Clore G.M., Gronenborn A.M. NMR and X-ray analysis of the three-dimensional structure of interleukin-8. Cytokines. 4:1992;18-40
    • (1992) Cytokines , vol.4 , pp. 18-40
    • Clore, G.M.1    Gronenborn, A.M.2
  • 6
    • 0023665258 scopus 로고
    • The yeast ribosomal protein L32 and its gene
    • Dabeva M.D., Warner J.R. The yeast ribosomal protein L32 and its gene. J. Biol. Chem. 262:1987;16055-16059
    • (1987) J. Biol. Chem. , vol.262 , pp. 16055-16059
    • Dabeva, M.D.1    Warner, J.R.2
  • 7
    • 0027305846 scopus 로고
    • Ribosomal protein L32 of Saccharomyces cerevisiae regulates both splicing and translation of its own transcript
    • Dabeva M.D., Warner J.R. Ribosomal protein L32 of Saccharomyces cerevisiae regulates both splicing and translation of its own transcript. J. Biol. Chem. 268:1993;19669-19674
    • (1993) J. Biol. Chem. , vol.268 , pp. 19669-19674
    • Dabeva, M.D.1    Warner, J.R.2
  • 8
    • 0022476239 scopus 로고
    • Autogenous regulation of splicing of the transcript of a yeast ribosomal protein gene
    • Dabeva M.D., Post-Beittenmiller M.A., Warner J.R. Autogenous regulation of splicing of the transcript of a yeast ribosomal protein gene. Proc. Natl. Acad. Sci. USA. 83:1986;5854-5857
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5854-5857
    • Dabeva, M.D.1    Post-Beittenmiller, M.A.2    Warner, J.R.3
  • 10
    • 0025827734 scopus 로고
    • Structural basis for the regulation of splicing of a yeast messenger RNA
    • Eng F.J., Warner J.R. Structural basis for the regulation of splicing of a yeast messenger RNA. Cell. 65:1991;797-804
    • (1991) Cell , vol.65 , pp. 797-804
    • Eng, F.J.1    Warner, J.R.2
  • 11
    • 0030596154 scopus 로고    scopus 로고
    • Ribosomal protein L9: A structure determination by the combined use of X-ray crystallography and NMR spectroscopy
    • Hoffman D.W., Cameron C.S., Davies C., White S.W., Ramakrishnan V. Ribosomal protein L9. a structure determination by the combined use of X-ray crystallography and NMR spectroscopy J. Mol. Biol. 264:1996;1058-1071
    • (1996) J. Mol. Biol. , vol.264 , pp. 1058-1071
    • Hoffman, D.W.1    Cameron, C.S.2    Davies, C.3    White, S.W.4    Ramakrishnan, V.5
  • 13
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A. The kink-turn. a new RNA secondary structure motif EMBO J. 20:2001;4214-4221
    • (2001) EMBO J. , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 15
    • 0030614970 scopus 로고    scopus 로고
    • RNA apatamers for yeast ribosomal protein L32 have a conserved purine-rich internal loop
    • Li H., White S.A. RNA apatamers for yeast ribosomal protein L32 have a conserved purine-rich internal loop. RNA. 3:1997;245-254
    • (1997) RNA , vol.3 , pp. 245-254
    • Li, H.1    White, S.A.2
  • 16
    • 0029143120 scopus 로고
    • Characterization of the pre-mRNA binding site for yeast ribosomal protein L32: The importance of a purine-rich internal loop
    • Li H., Dalal S., Kohler J., Vilardell J., White S.A. Characterization of the pre-mRNA binding site for yeast ribosomal protein L32. the importance of a purine-rich internal loop J. Mol. Biol. 250:1995;447-459
    • (1995) J. Mol. Biol. , vol.250 , pp. 447-459
    • Li, H.1    Dalal, S.2    Kohler, J.3    Vilardell, J.4    White, S.A.5
  • 17
    • 0029965321 scopus 로고    scopus 로고
    • An RNA structure involved in feedback regulation of splicing and of translation is critical for biological fitness
    • Li B., Vilardell J., Warner J.R. An RNA structure involved in feedback regulation of splicing and of translation is critical for biological fitness. Proc. Natl. Acad. Sci. USA. 93:1996;1596-1600
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1596-1600
    • Li, B.1    Vilardell, J.2    Warner, J.R.3
  • 18
    • 0035119966 scopus 로고    scopus 로고
    • Pulse sequences for detection of NH2.N hydrogen bonds in sheared G . a mismatches via remote, non-exchangeable protons
    • Majumdar A., Kettani A., Skripkin E., Patel D.J. Pulse sequences for detection of NH2.N hydrogen bonds in sheared G. A mismatches via remote, non-exchangeable protons. J. Biomol. NMR. 19:2001;103-113
    • (2001) J. Biomol. NMR , vol.19 , pp. 103-113
    • Majumdar, A.1    Kettani, A.2    Skripkin, E.3    Patel, D.J.4
  • 20
    • 0345035248 scopus 로고    scopus 로고
    • Assignment of the L30-mRNA complex using selective isotopic labeling and RNA mutants
    • a
    • Mao H., Williamson J.R. Assignment of the L30-mRNA complex using selective isotopic labeling and RNA mutants. Nucleic Acids Res. 27:1999;4059-4070. a
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4059-4070
    • Mao, H.1    Williamson, J.R.2
  • 21
    • 0033578955 scopus 로고    scopus 로고
    • Local folding coupled to RNA binding in the yeast ribosomal protein L30
    • b
    • Mao H., Williamson J.R. Local folding coupled to RNA binding in the yeast ribosomal protein L30. J. Mol. Biol. 292:1999;345-359. b
    • (1999) J. Mol. Biol. , vol.292 , pp. 345-359
    • Mao, H.1    Williamson, J.R.2
  • 22
    • 0032710024 scopus 로고    scopus 로고
    • A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex
    • Mao H., White S.A., Williamson J.R. A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex. Nat. Struct. Biol. 6:1999;1139-1147
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1139-1147
    • Mao, H.1    White, S.A.2    Williamson, J.R.3
  • 23
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit. a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125:1999;156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 24
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 26
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallogr. D Biol. Crystallogr. 57:2001;1367-1372
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 27
    • 0029633186 scopus 로고
    • AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules
    • Pearlman D.A., Case D.A., Caldwell J.W., Ross W.R., Cheatham T.E. III, DeBolt S., Ferguson D., Seibel G., Kollman P. AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comput. Phys. Commun. 91:1995;1-41
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.R.4    Cheatham III, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 28
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho F.A., Spurlino J.C., Rodseth L.E. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure. 5:1997;997-1015
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 29
    • 0035211933 scopus 로고    scopus 로고
    • Joint refinement as a tool for thorough comparison between NMR and X- ray data and structures of HU protein
    • Raves M.L., Doreleijer J.F., Vis H., Vorgias C.E., Wilson K.S., Kaptei R. Joint refinement as a tool for thorough comparison between NMR and X- ray data and structures of HU protein. J. Biomol. NMR. 21:2001;235-248
    • (2001) J. Biomol. NMR , vol.21 , pp. 235-248
    • Raves, M.L.1    Doreleijer, J.F.2    Vis, H.3    Vorgias, C.E.4    Wilson, K.S.5    Kaptei, R.6
  • 30
    • 0027983623 scopus 로고
    • Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals
    • Schiffer C.A., Huber R., Wuthrich K., van Gunsteren W.F. Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals. J. Mol. Biol. 241:1994;588-599
    • (1994) J. Mol. Biol. , vol.241 , pp. 588-599
    • Schiffer, C.A.1    Huber, R.2    Wuthrich, K.3    Van Gunsteren, W.F.4
  • 31
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment
    • Vidovic I., Nottrott S., Hartmuth K., Luhrmann R., Ficner R. Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment. Mol. Cell. 6:2000;1331-1342
    • (2000) Mol. Cell , vol.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Hartmuth, K.3    Luhrmann, R.4    Ficner, R.5
  • 32
    • 0027957734 scopus 로고
    • Regulation of splicing at an intermediate step in the formation of the spliceosome
    • Vilardell J., Warner J.R. Regulation of splicing at an intermediate step in the formation of the spliceosome. Genes Dev. 8:1994;211-220
    • (1994) Genes Dev. , vol.8 , pp. 211-220
    • Vilardell, J.1    Warner, J.R.2
  • 33
    • 0029805283 scopus 로고    scopus 로고
    • Yeast ribosomal protein L32 recognizes an RNA G:U juxtaposition
    • White S.A., Li H. Yeast ribosomal protein L32 recognizes an RNA G:U juxtaposition. RNA. 2:1996;226-234
    • (1996) RNA , vol.2 , pp. 226-234
    • White, S.A.1    Li, H.2
  • 34
    • 0034897731 scopus 로고    scopus 로고
    • The GA motif: An RNA element common to bacterial antitermination systems, rRNA, and eukaryotic RNAs
    • Winkler W.C., Grundy F.J., Murphy B.A., Henkin T.M. The GA motif. an RNA element common to bacterial antitermination systems, rRNA, and eukaryotic RNAs RNA. 7:2001;1165-1172
    • (2001) RNA , vol.7 , pp. 1165-1172
    • Winkler, W.C.1    Grundy, F.J.2    Murphy, B.A.3    Henkin, T.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.