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Volumn 14, Issue 6, 2005, Pages 1472-1484

Structural and functional characterization of CFE88: Evidence that a conserved and essential bacterial protein is a methyltransferase

Author keywords

Bioinformatics; Biophysical methods; Conserved essential bacterial gene; Methyltransferase; Mutagenesis; Nuclear magnetic resonance; Protein modeling; Streptococcus pneumoniae

Indexed keywords

BACTERIAL PROTEIN; CARBON; GENE PRODUCT; METHYLTRANSFERASE; NITROGEN; S ADENOSYLHOMOCYSTEINE;

EID: 22444432137     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051389605     Document Type: Article
Times cited : (4)

References (53)
  • 5
    • 0026705492 scopus 로고
    • Epidemiology of drug resistance: Implications for a post-antimicrobial era
    • Cohen, M.J. 1992. Epidemiology of drug resistance: Implications for a post-antimicrobial era. Science 257: 1050-1055.
    • (1992) Science , vol.257 , pp. 1050-1055
    • Cohen, M.J.1
  • 7
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies, J. 1994. Inactivation of antibiotics and the dissemination of resistance genes. Science 264: 375-382.
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 8
    • 0025149607 scopus 로고
    • Multiple mechanisms of erythromycin resistance
    • Eady, E.A., Ross, J.I., and Cove, J.H. 1990. Multiple mechanisms of erythromycin resistance. Antimicrob. Chemother. 26: 461-471.
    • (1990) Antimicrob. Chemother. , vol.26 , pp. 461-471
    • Eady, E.A.1    Ross, J.I.2    Cove, J.H.3
  • 10
    • 32744457796 scopus 로고
    • Frameshift: A rigorous alignment program for searching protein databases with nucleic acid queries
    • Hilton Head, SC
    • Edelman, I., Faigler, S., Mintz, E., Natan, A., and Devereux, J. 1995. Frameshift: A rigorous alignment program for searching protein databases with nucleic acid queries. Genome Sequence and Analysis Conference. Hilton Head, SC.
    • (1995) Genome Sequence and Analysis Conference
    • Edelman, I.1    Faigler, S.2    Mintz, E.3    Natan, A.4    Devereux, J.5
  • 11
    • 0028502038 scopus 로고
    • 15N]-separated 4D gradient-enhanced NOESY spectra in proteins
    • 15N]-separated 4D gradient-enhanced NOESY spectra in proteins. J. Biomol. NMR 4: 673-687.
    • (1994) J. Biomol. NMR , vol.4 , pp. 673-687
    • Farmer II, B.T.1    Mueller, L.2
  • 13
    • 0031297326 scopus 로고    scopus 로고
    • Protein folds from pair interactions: A blind test in fold recognition
    • Flockner, H., Domingues, F.S., and Sippl, M.J. 1997. Protein folds from pair interactions: A blind test in fold recognition. Proteins 1: 129-133.
    • (1997) Proteins , vol.1 , pp. 129-133
    • Flockner, H.1    Domingues, F.S.2    Sippl, M.J.3
  • 15
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. 1992. Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114: 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 17
    • 0034611088 scopus 로고    scopus 로고
    • Design and synthesis of mimics of S-adenosyl-L-homocysteine as potential inhibitors of erythromycin methyltransferase
    • Hanessian, S. and Sgarbi, P. W. 2000. Design and synthesis of mimics of S-adenosyl-L-homocysteine as potential inhibitors of erythromycin methyltransferase. Bioorg. Med. Chem. Lett. 10: 433-437.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 433-437
    • Hanessian, S.1    Sgarbi, P.W.2
  • 18
    • 32744465812 scopus 로고    scopus 로고
    • Finding homologs to nucleic acid or protein sequences using the FrameSearch program
    • eds. Baxevanis et al. John Wiley & Sons, NY.
    • Healy, M.D. 2003. Finding homologs to nucleic acid or protein sequences using the FrameSearch program. In Current Protocols in Bioinformatics. (eds. Baxevanis et al.) pp. 3.2.1-3.2.23. John Wiley & Sons, NY.
    • (2003) Current Protocols in Bioinformatics
    • Healy, M.D.1
  • 19
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D.G., Thompson, J.D., and Gibson, T.J. 1996. Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266: 383-402.
    • (1996) Methods Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 20
    • 3242813635 scopus 로고    scopus 로고
    • Utility of homology models in the drug discovery process
    • Hillisch, A., Pineda, L.F., and Hilgenfeld, R. 2004. Utility of homology models in the drug discovery process. Drug Disc. Today 9: 659-669.
    • (2004) Drug Disc. Today , vol.9 , pp. 659-669
    • Hillisch, A.1    Pineda, L.F.2    Hilgenfeld, R.3
  • 21
    • 0347761359 scopus 로고    scopus 로고
    • NMR spectroscopy tools for structure-aided drug design
    • Homans, S.W. 2004. NMR spectroscopy tools for structure-aided drug design. Angew. Chem. Int. Ed. 43: 290-300.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 290-300
    • Homans, S.W.1
  • 22
    • 0006925492 scopus 로고
    • Pure absorption gradient-enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P., and Saarinen, T. 1992. Pure absorption gradient-enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114: 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 25
    • 0036716799 scopus 로고    scopus 로고
    • Resistance to macrolides and related antibiotics in Streptococcus pneumoniae
    • Leclercq, R. and Courvalin, P. 2002. Resistance to macrolides and related antibiotics in Streptococcus pneumoniae. Antimicrob. Agents Chemother. 46: 2727-2734.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2727-2734
    • Leclercq, R.1    Courvalin, P.2
  • 26
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt, M. 1992. Accurate modeling of protein conformation by automatic segment matching. J. Mol. Biol. 226: 507-533.
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 27
    • 0026619586 scopus 로고
    • Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments
    • Logan, T.M., Olejniczak, E.T., Xu, R.X., and Fesik, S.W. 1992. Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments. FEBS Lett. 314: 413-418.
    • (1992) FEBS Lett. , vol.314 , pp. 413-418
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 29
    • 0030137565 scopus 로고    scopus 로고
    • Use of selective Cα pulses for improvement of HN(CA)CO-D and HN(CACO)NH-D experiments
    • Matsuo, H., Kupce, E., Li, J., and Wagner, G. 1996. Use of selective Cα pulses for improvement of HN(CA)CO-D and HN(CACO)NH-D experiments. J. Magn. Reson. B 111: 194-198.
    • (1996) J. Magn. Reson. B , vol.111 , pp. 194-198
    • Matsuo, H.1    Kupce, E.2    Li, J.3    Wagner, G.4
  • 32
    • 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
  • 33
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. 1994. Prevention of drug access to bacterial targets: Permeability barriers and active efflux. Science 264: 382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 37
    • 0029795692 scopus 로고    scopus 로고
    • Competence for genetic transformation in encapsulated strains of Streptococcus pneumoniae: Two allelic variants of the peptide pheromone
    • Pozzi, G., Masala, L., Iannelli, F., Manganelli, R., Havarstein, L.S., Piccoli, L., Simon, D., and Morrison, D.A. 1996. Competence for genetic transformation in encapsulated strains of Streptococcus pneumoniae: Two allelic variants of the peptide pheromone. J. Bacteriol. 178: 6087-6090.
    • (1996) J. Bacteriol. , vol.178 , pp. 6087-6090
    • Pozzi, G.1    Masala, L.2    Iannelli, F.3    Manganelli, R.4    Havarstein, L.S.5    Piccoli, L.6    Simon, D.7    Morrison, D.A.8
  • 38
    • 0033522646 scopus 로고    scopus 로고
    • The 2.2 Å structure of the rRNA methyltransfease ErmC′ and its complexes with cofactor and cofactor analogs: Implications for the reaction mechanism
    • Schluckebier, G., Zhong, P., Stewart, K.D., Kavanaugh, T.J., and Abad-Zapatero, C. 1999. The 2.2 Å structure of the rRNA methyltransfease ErmC′ and its complexes with cofactor and cofactor analogs: Implications for the reaction mechanism. J. Mol. Biol. 289: 277-291.
    • (1999) J. Mol. Biol. , vol.289 , pp. 277-291
    • Schluckebier, G.1    Zhong, P.2    Stewart, K.D.3    Kavanaugh, T.J.4    Abad-Zapatero, C.5
  • 40
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T.F. and Waterman, M.S. 1981. Identification of common molecular subsequences. J. Mol. Biol. 147: 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 41
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E.L, Eddy, S.R., and Durbin, R. 1997. Pfam: A comprehensive database of protein domain families based on seed alignments. Proteins 28: 405-420.
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 42
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113: 5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, A.1    Bax, A.2
  • 43
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B.G. 1994. Resistance to antibiotics mediated by target alterations. Science 264: 388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 44
    • 0037100683 scopus 로고    scopus 로고
    • Identification of 113 conserved essential genes using a high-throughput gene disruption system in Streptococcus pneumoniae
    • Thanassi, J.A., Hartman-Neumann, S.L., Dougherty, T.J., Dougherty, B.A., and Pucci, M.J. 2002. Identification of 113 conserved essential genes using a high-throughput gene disruption system in Streptococcus pneumoniae. Nucleic Acids Res. 30: 3152-3162.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3152-3162
    • Thanassi, J.A.1    Hartman-Neumann, S.L.2    Dougherty, T.J.3    Dougherty, B.A.4    Pucci, M.J.5
  • 47
    • 0013498057 scopus 로고
    • 13C separated HMQC-NOESY-HMQC spectra using pulsed field gradients
    • 13C separated HMQC-NOESY-HMQC spectra using pulsed field gradients. J. Magn. Reson. ser. B 101: 210-213.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 210-213
    • Vuister, G.W.1    Bax, A.2
  • 48
    • 0345839252 scopus 로고    scopus 로고
    • Where will new antibiotics come from?
    • Walsh, C. 2003. Where will new antibiotics come from? Nat. Rev. Microbiol. 1: 65-70.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 65-70
    • Walsh, C.1
  • 49
    • 32744457668 scopus 로고    scopus 로고
    • New fungal nucleic acids and polypeptides, useful in diagnosing, preventing, treating or ameliorating fungal infection or infectious disease, eliciting an immune response or in drug screening. Patent WO2003091418-A2 (Publication date: 06 November 2003; Filing date: 25 April 2003; 2003WO-US013081)
    • Wang, Y., Liu, M., Dougherty, B.A., Healy, M.D., Davison, D.B., Mazzucco, C.E., Krystek, S.R., and Bassolino, D.A. 2003. New fungal nucleic acids and polypeptides, useful in diagnosing, preventing, treating or ameliorating fungal infection or infectious disease, eliciting an immune response or in drug screening. Patent WO2003091418-A2 (Publication date: 06 November 2003; Filing date: 25 April 2003; 2003WO-US013081).
    • (2003)
    • Wang, Y.1    Liu, M.2    Dougherty, B.A.3    Healy, M.D.4    Davison, D.B.5    Mazzucco, C.E.6    Krystek, S.R.7    Bassolino, D.A.8
  • 50
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum, B. 1995. Erythromycin resistance by ribosome modification. Antimicrob. Chemother. 39: 577-585.
    • (1995) Antimicrob. Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 51
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shifts and secondary structure
    • Wishart, D.S. and Sykes, B.D. 1991. Relationship between nuclear magnetic resonance chemical shifts and secondary structure. J. Mol. Biol. 222: 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2
  • 52
    • 0030902818 scopus 로고    scopus 로고
    • Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance
    • Yu, L., Petros, A.M., Schnuchel, A., Zhong, P., Severin, J.M., Walter, K., Holszman, T.F., and Fesik, S.W. 1997. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat. Struct. Biol. 4: 483-489.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 483-489
    • Yu, L.1    Petros, A.M.2    Schnuchel, A.3    Zhong, P.4    Severin, J.M.5    Walter, K.6    Holszman, T.F.7    Fesik, S.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.