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Volumn 49, Issue 30, 2010, Pages 6440-6450

Crystal structure of the nosiheptide-resistance methyltransferase of streptomyces actuosus

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ANALYSIS; CATALYTIC DOMAINS; CATALYTIC MECHANISMS; CRITICAL REGION; HOMODIMERS; METHYL GROUP; METHYLTRANSFERASE ACTIVITY; METHYLTRANSFERASES; N-TERMINALS; PEPTIDE ANTIBIOTICS; RNA BINDING DOMAINS; RNA RECOGNITION; RNA SUBSTRATE; S ADENOSYL L METHIONINES; STRUCTURAL MODELS; STRUCTURAL STUDIES; SUBSTRATE RECOGNITION;

EID: 77955026872     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1005915     Document Type: Article
Times cited : (14)

References (48)
  • 2
    • 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., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289, 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
  • 5
    • 0036791606 scopus 로고    scopus 로고
    • The bacterial ribosome, a promising focus for structure-based drug design
    • Knowles, D. J., Foloppe, N., Matassova, N. B., and Murchie, A. I. (2002) The bacterial ribosome, a promising focus for structure-based drug design Curr. Opin. Pharmacol. 2, 501-506
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 501-506
    • Knowles, D.J.1    Foloppe, N.2    Matassova, N.B.3    Murchie, A.I.4
  • 6
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. (2002) Ribosome structure and the mechanism of translation Cell 108, 557-572
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 7
    • 0033966335 scopus 로고    scopus 로고
    • The macrolide-lincosamide-streptogramin B resistance determinant from Clostridium difficile 630 contains two erm(B) genes
    • Farrow, K. A., Lyras, D., and Rood, J. I. (2000) The macrolide- lincosamide-streptogramin B resistance determinant from Clostridium difficile 630 contains two erm(B) genes Antimicrob. Agents Chemother. 44, 411-413
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 411-413
    • Farrow, K.A.1    Lyras, D.2    Rood, J.I.3
  • 8
    • 0028076141 scopus 로고
    • 23S rRNA domain V, a fragment that can be specifically methylated in vitro by the ErmSF (TlrA) methyltransferase
    • Kovalic, D., Giannattasio, R. B., Jin, H. J., and Weisblum, B. (1994) 23S rRNA domain V, a fragment that can be specifically methylated in vitro by the ErmSF (TlrA) methyltransferase J. Bacteriol. 176, 6992-6998
    • (1994) J. Bacteriol. , vol.176 , pp. 6992-6998
    • Kovalic, D.1    Giannattasio, R.B.2    Jin, H.J.3    Weisblum, B.4
  • 9
    • 0028035257 scopus 로고
    • Domain v of 23S rRNA contains all the structural elements necessary for recognition by the ErmE methyltransferase
    • Vester, B. and Douthwaite, S. (1994) Domain V of 23S rRNA contains all the structural elements necessary for recognition by the ErmE methyltransferase J. Bacteriol. 176, 6999-7004
    • (1994) J. Bacteriol. , vol.176 , pp. 6999-7004
    • Vester, B.1    Douthwaite, S.2
  • 10
    • 0027324801 scopus 로고
    • Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin) producer, Micromonospora olivasterospora: Comparison with other aminoglycoside-resistance-encoding genes
    • Ohta, T. and Hasegawa, M. (1993) Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin) producer, Micromonospora olivasterospora: comparison with other aminoglycoside-resistance-encoding genes Gene 127, 63-69
    • (1993) Gene , vol.127 , pp. 63-69
    • Ohta, T.1    Hasegawa, M.2
  • 11
    • 9644281537 scopus 로고    scopus 로고
    • Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes
    • Mosbacher, T. G., Bechthold, A., and Schulz, G. E. (2005) Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes J. Mol. Biol. 345, 535-545
    • (2005) J. Mol. Biol. , vol.345 , pp. 535-545
    • Mosbacher, T.G.1    Bechthold, A.2    Schulz, G.E.3
  • 12
    • 0036774065 scopus 로고    scopus 로고
    • The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot
    • Michel, G., Sauve, V., Larocque, R., Li, Y., Matte, A., and Cygler, M. (2002) The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot Structure 10, 1303-1315
    • (2002) Structure , vol.10 , pp. 1303-1315
    • Michel, G.1    Sauve, V.2    Larocque, R.3    Li, Y.4    Matte, A.5    Cygler, M.6
  • 13
    • 0042415065 scopus 로고    scopus 로고
    • Structural basis for contrasting activities of ribosome binding thiazole antibiotics
    • Lentzen, G., Klinck, R., Matassova, N., Aboul-ela, F., and Murchie, A. I. (2003) Structural basis for contrasting activities of ribosome binding thiazole antibiotics Chem. Biol. 10, 769-778
    • (2003) Chem. Biol. , vol.10 , pp. 769-778
    • Lentzen, G.1    Klinck, R.2    Matassova, N.3    Aboul-Ela, F.4    Murchie, A.I.5
  • 14
    • 0027933451 scopus 로고
    • Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA
    • Bechthold, A. and Floss, H. G. (1994) Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′- methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA Eur. J. Biochem. 224, 431-437
    • (1994) Eur. J. Biochem. , vol.224 , pp. 431-437
    • Bechthold, A.1    Floss, H.G.2
  • 15
    • 67650544978 scopus 로고    scopus 로고
    • Structure of the thiostrepton resistance methyltransferase S -adenosyl- l -methionine complex and its interaction with ribosomal RNA
    • Dunstan, M. S., Hang, P. C., Zelinskaya, N. V., Honek, J. F., and Conn, G. L. (2009) Structure of the thiostrepton resistance methyltransferase S -adenosyl- l -methionine complex and its interaction with ribosomal RNA J. Biol. Chem. 284, 17013-17020
    • (2009) J. Biol. Chem. , vol.284 , pp. 17013-17020
    • Dunstan, M.S.1    Hang, P.C.2    Zelinskaya, N.V.3    Honek, J.F.4    Conn, G.L.5
  • 16
    • 0020419248 scopus 로고
    • Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton
    • Thompson, J., Schmidt, F., and Cundliffe, E. (1982) Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton J. Biol. Chem. 257, 7915-7917
    • (1982) J. Biol. Chem. , vol.257 , pp. 7915-7917
    • Thompson, J.1    Schmidt, F.2    Cundliffe, E.3
  • 17
    • 0024286238 scopus 로고
    • Molecular cloning of the nosiheptide resistance gene from Streptomyces actuosus ATCC 25421
    • Dosch, D. C., Strohl, W. R., and Floss, H. G. (1988) Molecular cloning of the nosiheptide resistance gene from Streptomyces actuosus ATCC 25421 Biochem. Biophys. Res. Commun. 156, 517-523
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 517-523
    • Dosch, D.C.1    Strohl, W.R.2    Floss, H.G.3
  • 18
    • 0025045648 scopus 로고
    • Nucleotide sequence and transcriptional analysis of the nosiheptide-resistance gene from Streptomyces actuosus
    • Li, Y., Dosch, D. C., Strohl, W. R., and Floss, H. G. (1990) Nucleotide sequence and transcriptional analysis of the nosiheptide-resistance gene from Streptomyces actuosus Gene 91, 9-17
    • (1990) Gene , vol.91 , pp. 9-17
    • Li, Y.1    Dosch, D.C.2    Strohl, W.R.3    Floss, H.G.4
  • 19
    • 0017622981 scopus 로고
    • Structure of nosipeptide, a polythiazole-containing antibiotic
    • Prange, T., Ducruix, A., Pascard, C., and Lunel, J. (1977) Structure of nosipeptide, a polythiazole-containing antibiotic Nature 265, 189-190
    • (1977) Nature , vol.265 , pp. 189-190
    • Prange, T.1    Ducruix, A.2    Pascard, C.3    Lunel, J.4
  • 20
    • 0017849791 scopus 로고
    • Identity of multhiomycin with nosiheptide
    • Endo, T. and Yonehara, H. (1978) Identity of multhiomycin with nosiheptide J. Antibiot. (Tokyo) 31, 623-625
    • (1978) J. Antibiot. (Tokyo) , vol.31 , pp. 623-625
    • Endo, T.1    Yonehara, H.2
  • 21
    • 0021523913 scopus 로고
    • Efficacy of nosiheptide as a growth promotant for growing-finishing swine - A cooperative study
    • Cromwell, G. L., Stahly, T. S., Speer, V. C., and OKelly, R. (1984) Efficacy of nosiheptide as a growth promotant for growing-finishing swine - a cooperative study J. Anim. Sci. 59, 1125-1128
    • (1984) J. Anim. Sci. , vol.59 , pp. 1125-1128
    • Cromwell, G.L.1    Stahly, T.S.2    Speer, V.C.3    Okelly, R.4
  • 23
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • Cameron, D. M., Thompson, J., March, P. E., and Dahlberg, A. E. (2002) Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome J. Mol. Biol. 319, 27-35
    • (2002) J. Mol. Biol. , vol.319 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 24
    • 0033553439 scopus 로고    scopus 로고
    • A detailed view of a ribosomal active site: The structure of the L11-RNA complex
    • Wimberly, B. T., Guymon, R., McCutcheon, J. P., White, S. W., and Ramakrishnan, V. (1999) A detailed view of a ribosomal active site: the structure of the L11-RNA complex Cell 97, 491-502
    • (1999) Cell , vol.97 , pp. 491-502
    • Wimberly, B.T.1    Guymon, R.2    McCutcheon, J.P.3    White, S.W.4    Ramakrishnan, V.5
  • 25
    • 41549163979 scopus 로고    scopus 로고
    • Translational regulation via L11: Molecular switches on the ribosome turned on and off by thiostrepton and micrococcin
    • Harms, J. M., Wilson, D. N., Schluenzen, F., Connell, S. R., Stachelhaus, T., Zaborowska, Z., Spahn, C. M., and Fucini, P. (2008) Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin Mol. Cell 30, 26-38
    • (2008) Mol. Cell , vol.30 , pp. 26-38
    • Harms, J.M.1    Wilson, D.N.2    Schluenzen, F.3    Connell, S.R.4    Stachelhaus, T.5    Zaborowska, Z.6    Spahn, C.M.7    Fucini, P.8
  • 27
    • 0025330496 scopus 로고
    • Characterization of the binding sites of protein L11 and the L10-(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coli
    • Egebjerg, J., Douthwaite, S. R., Liljas, A., and Garrett, R. A. (1990) Characterization of the binding sites of protein L11 and the L10-(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coli J. Mol. Biol. 213, 275-288
    • (1990) J. Mol. Biol. , vol.213 , pp. 275-288
    • Egebjerg, J.1    Douthwaite, S.R.2    Liljas, A.3    Garrett, R.A.4
  • 28
    • 33846916194 scopus 로고    scopus 로고
    • L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy
    • Jonker, H. R., Ilin, S., Grimm, S. K., Wohnert, J., and Schwalbe, H. (2007) L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy Nucleic Acids Res. 35, 441-454
    • (2007) Nucleic Acids Res. , vol.35 , pp. 441-454
    • Jonker, H.R.1    Ilin, S.2    Grimm, S.K.3    Wohnert, J.4    Schwalbe, H.5
  • 29
    • 0019810825 scopus 로고
    • The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli
    • Schmidt, F. J., Thompson, J., Lee, K., Dijk, J., and Cundliffe, E. (1981) The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli J. Biol. Chem. 256, 12301-12305
    • (1981) J. Biol. Chem. , vol.256 , pp. 12301-12305
    • Schmidt, F.J.1    Thompson, J.2    Lee, K.3    Dijk, J.4    Cundliffe, E.5
  • 30
    • 0033553625 scopus 로고    scopus 로고
    • Crystal structure of a conserved ribosomal protein-RNA complex
    • Conn, G. L., Draper, D. E., Lattman, E. E., and Gittis, A. G. (1999) Crystal structure of a conserved ribosomal protein-RNA complex Science 284, 1171-1174
    • (1999) Science , vol.284 , pp. 1171-1174
    • Conn, G.L.1    Draper, D.E.2    Lattman, E.E.3    Gittis, A.G.4
  • 31
    • 0028261409 scopus 로고
    • Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective
    • Gutell, R. R., Larsen, N., and Woese, C. R. (1994) Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective Microbiol. Rev. 58, 10-26
    • (1994) Microbiol. Rev. , vol.58 , pp. 10-26
    • Gutell, R.R.1    Larsen, N.2    Woese, C.R.3
  • 32
    • 0028231009 scopus 로고
    • The bacterial nucleoid revisited
    • Robinow, C. and Kellenberger, E. (1994) The bacterial nucleoid revisited Microbiol. Rev. 58, 211-232
    • (1994) Microbiol. Rev. , vol.58 , pp. 211-232
    • Robinow, C.1    Kellenberger, E.2
  • 33
    • 0029832294 scopus 로고    scopus 로고
    • Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes
    • Gustafsson, C., Reid, R., Greene, P. J., and Santi, D. V. (1996) Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes Nucleic Acids Res. 24, 3756-3762
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3756-3762
    • Gustafsson, C.1    Reid, R.2    Greene, P.J.3    Santi, D.V.4
  • 34
    • 33845919828 scopus 로고    scopus 로고
    • Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes
    • Watanabe, K., Nureki, O., Fukai, S., Endo, Y., and Hori, H. (2006) Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes J. Biol. Chem. 281, 34630-34639
    • (2006) J. Biol. Chem. , vol.281 , pp. 34630-34639
    • Watanabe, K.1    Nureki, O.2    Fukai, S.3    Endo, Y.4    Hori, H.5
  • 35
    • 0141592367 scopus 로고    scopus 로고
    • Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 Å resolution: A novel methyltransferase fold
    • Liu, J., Wang, W., Shin, D. H., Yokota, H., Kim, R., and Kim, S. H. (2003) Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 Å resolution: a novel methyltransferase fold Proteins 53, 326-328
    • (2003) Proteins , vol.53 , pp. 326-328
    • Liu, J.1    Wang, W.2    Shin, D.H.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 37
    • 15444370839 scopus 로고    scopus 로고
    • Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family
    • Watanabe, K., Nureki, O., Fukai, S., Ishii, R., Okamoto, H., Yokoyama, S., Endo, Y., and Hori, H. (2005) Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family J. Biol. Chem. 280, 10368-10377
    • (2005) J. Biol. Chem. , vol.280 , pp. 10368-10377
    • Watanabe, K.1    Nureki, O.2    Fukai, S.3    Ishii, R.4    Okamoto, H.5    Yokoyama, S.6    Endo, Y.7    Hori, H.8
  • 38
    • 77952001676 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of nosiheptide-resistance methyltransferase from Streptomyces actuosus in complex with SAM
    • Yang, H., Wang, P., Dong, Z., Li, X., Gong, R., Yang, Y., Li, Z., Xu, Y., and Xu, Y. (2010) Crystallization and preliminary crystallographic analysis of nosiheptide-resistance methyltransferase from Streptomyces actuosus in complex with SAM Acta Crystallogr. 66, 579-582
    • (2010) Acta Crystallogr. , vol.66 , pp. 579-582
    • Yang, H.1    Wang, P.2    Dong, Z.3    Li, X.4    Gong, R.5    Yang, Y.6    Li, Z.7    Xu, Y.8    Xu, Y.9
  • 39
    • 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
    • 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
  • 43
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3 Bioinformatics 24, 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 44
  • 45
    • 3142608984 scopus 로고    scopus 로고
    • Joint X-ray and NMR refinement of the yeast L30e-mRNA complex
    • Chao, J. A. and Williamson, J. R. (2004) Joint X-ray and NMR refinement of the yeast L30e-mRNA complex Structure 12, 1165-1176
    • (2004) Structure , vol.12 , pp. 1165-1176
    • Chao, J.A.1    Williamson, J.R.2
  • 47
    • 2342638215 scopus 로고    scopus 로고
    • Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution
    • Hamma, T. and Ferre-D'Amare, A. R. (2004) Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution Structure 12, 893-903
    • (2004) Structure , vol.12 , pp. 893-903
    • Hamma, T.1    Ferre-D'amare, A.R.2
  • 48
    • 0018351356 scopus 로고
    • Ribose methylation and resistance to thiostrepton
    • Cundliffe, E. and Thompson, J. (1979) Ribose methylation and resistance to thiostrepton Nature 278, 859-861
    • (1979) Nature , vol.278 , pp. 859-861
    • Cundliffe, E.1    Thompson, J.2


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