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Volumn 289, Issue 2, 1999, Pages 277-291

The 2.2 Å structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: Implications for the reaction mechanism

Author keywords

Antibiotic resistance; Methyltransferase; S adenosyl L methionine; Sinefungin; X ray structure

Indexed keywords

ADENINE; AMINO ACID; ENZYME INHIBITOR; HOMOCYSTEINE; MACROLIDE; METHYLTRANSFERASE; RIBOSOME RNA; RNA 23S; RNA METHYLTRANSFERASE; S ADENOSYLMETHIONINE; SINEFUNGIN; TRANSFERASE; ADENOSINE; ANTIFUNGAL AGENT; DRUG DERIVATIVE; LIGAND; RRNA (ADENOSINE O 2' )METHYLTRANSFERASE; RRNA (ADENOSINE-O-2'-)METHYLTRANSFERASE; S ADENOSYLHOMOCYSTEINE;

EID: 0033522646     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2788     Document Type: Article
Times cited : (95)

References (41)
  • 2
    • 37049050461 scopus 로고
    • The methylation of adenosine and adenylic acid
    • Brookes P., Lawley P. D. The methylation of adenosine and adenylic acid. J. Chem. Soc. 1960;539-545.
    • (1960) J. Chem. Soc. , pp. 539-545
    • Brookes, P.1    Lawley, P.D.2
  • 3
    • 0003769049 scopus 로고
    • New Haven and London: Yale University Press
    • Brünger A. T. X-PLOR Version 3.1. 1992;Yale University Press, New Haven and London.
    • (1992) X-PLOR Version 3.1
    • Brünger, A.T.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Ccp4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 8
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction
    • Cheng Y.-P., Prusoff W. H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction. Biochem. Pharmacol. 22:1973;3099-3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.-P.1    Prusoff, W.H.2
  • 11
    • 0024587767 scopus 로고
    • Mono- And dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase
    • Denoya C., Dubnau D. Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase. J. Biol. Chem. 264:1989;2615-2624.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2615-2624
    • Denoya, C.1    Dubnau, D.2
  • 12
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
    • Djordjevic S., Stock A. M. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure. 5:1997;545-558.
    • (1997) Structure , vol.5 , pp. 545-558
    • Djordjevic, S.1    Stock, A.M.2
  • 13
    • 0030612472 scopus 로고    scopus 로고
    • Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
    • Gong W., O'Gara M., Blumenthal R. M., Cheng X. Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. Nucl. Acids Res. 25:1997;2702-2715.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2702-2715
    • Gong, W.1    O'Gara, M.2    Blumenthal, R.M.3    Cheng, X.4
  • 14
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford P. J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28:1985;849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 15
    • 37049065738 scopus 로고
    • The methylation of nucleosides and mononucleotides with diazomethan
    • Haines J. A., Reese C. B., Todd L. The methylation of nucleosides and mononucleotides with diazomethan. J. Chem. Soc. 1964;1406-1412.
    • (1964) J. Chem. Soc. , pp. 1406-1412
    • Haines, J.A.1    Reese, C.B.2    Todd, L.3
  • 16
    • 0029665054 scopus 로고    scopus 로고
    • The 1.85 Å structure of vaccina protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends
    • Hodel A. E., Gershon P. D., Shi X., Quiocho F. A. The 1.85 Å structure of vaccina protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. Cell. 85:1996;247-256.
    • (1996) Cell , vol.85 , pp. 247-256
    • Hodel, A.E.1    Gershon, P.D.2    Shi, X.3    Quiocho, F.A.4
  • 17
    • 0024398664 scopus 로고
    • Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes: Common sequence motifs for protein DNA, RNA and small molecule S-adenosylmethionine dependent methyltransferases
    • Ingrosso D., Fowler A. V., Bleibaum J., Clarke S. Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes: common sequence motifs for protein DNA, RNA and small molecule S-adenosylmethionine dependent methyltransferases. J. Biol. Chem. 264:1989;20131-21039.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20131-21039
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 18
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt L. A., Wang J., Friedman J. M., Rice P. A., Steiz T. A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science. 256:1992;1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steiz, T.A.5
  • 19
    • 0028076141 scopus 로고
    • 23 S rRNA domain V, a fragment that can be specifically methylated in vitro by ErmSF (TlrA) methyltransferase
    • Kovalic D., Giannattasio R. B., Jin H. J., Weisblum B. 23 S rRNA domain V, a fragment that can be specifically methylated in vitro by ErmSF (TlrA) methyltransferase. J. Bacteriol. 176:1994;6992-6998.
    • (1994) J. Bacteriol. , vol.176 , pp. 6992-6998
    • Kovalic, D.1    Giannattasio, R.B.2    Jin, H.J.3    Weisblum, B.4
  • 20
    • 0028790412 scopus 로고
    • Methylation of minimalist 23 S rRNA sequences in vitro by ErmSF (TrlA) N-methyltransferase
    • Kovalic D., Giannattasio R. B., Weisblum B. Methylation of minimalist 23 S rRNA sequences in vitro by ErmSF (TrlA) N-methyltransferase. Biochemistry. 34:1995;15838-15844.
    • (1995) Biochemistry , vol.34 , pp. 15838-15844
    • Kovalic, D.1    Giannattasio, R.B.2    Weisblum, B.3
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M. TaqI in complex with the cofactor S-adenosylmethionine
    • Labahn J., Granzin J., Schluckebier G., Robinson D., Jack W., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M. TaqI in complex with the cofactor S-adenosylmethionine. Proc. Natl Acad. Sci. USA. 91:1994;10957-10961.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10957-10961
    • Labahn, J.1    Granzin, J.2    Schluckebier, G.3    Robinson, D.4    Jack, W.5    Schildkraut, I.6    Saenger, W.7
  • 23
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyl-transferases, and suggests a catalytic mechanism for these enzymes
    • Malone T., Blumenthal R., Cheng X. Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyl-transferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253:1995;618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.2    Cheng, X.3
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. D. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington: SERC Laboratory Daresbury
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend: Data Collection and Processing. 1993;56-62 SERC Laboratory Daresbury, Warrington.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 27
    • 0033514427 scopus 로고    scopus 로고
    • Functional roles of the conserved aromatic amino acid residues at position 108 (Motif IV) and position 196 (Motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus
    • Pues H., Bleimling N., Holz B., Woelcke J., Weinhold E. Functional roles of the conserved aromatic amino acid residues at position 108 (Motif IV) and position 196 (Motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus. Biochemistry. 38:1999;1426-1434.
    • (1999) Biochemistry , vol.38 , pp. 1426-1434
    • Pues, H.1    Bleimling, N.2    Holz, B.3    Woelcke, J.4    Weinhold, E.5
  • 28
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases form partial structures with errors
    • Read R. Improved Fourier coefficients for maps using phases form partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.1
  • 29
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann M., Moras D., Olsen K. Chemical and biological evolution of a nucleotide-binding protein. Nature. 250:1974;194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.1    Moras, D.2    Olsen, K.3
  • 30
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier G., O'Gara M., Saenger W., Cheng X. Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247:1995;16-20.
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 31
    • 0031561804 scopus 로고    scopus 로고
    • Differential binding of AdoMet, AdoHcy and Sinefungin to the adenine-specific DNA methyltransferase M. TaqI
    • Schluckebier G., Kozak M., Bleimling N., Weinhold E., Saenger W. Differential binding of AdoMet, AdoHcy and Sinefungin to the adenine-specific DNA methyltransferase M. TaqI. J. Mol. Biol. 265:1997;56-67.
    • (1997) J. Mol. Biol. , vol.265 , pp. 56-67
    • Schluckebier, G.1    Kozak, M.2    Bleimling, N.3    Weinhold, E.4    Saenger, W.5
  • 32
    • 0031959007 scopus 로고    scopus 로고
    • M. TaqI: Possible catalysis via cation-π interactions in N-specific DNA methyltransferases
    • Schluckebier G., Labahn J., Granzin J., Saenger W. M. TaqI: possible catalysis via cation-π interactions in N-specific DNA methyltransferases. J. Biol. Chem. 379:1998;389-400.
    • (1998) J. Biol. Chem. , vol.379 , pp. 389-400
    • Schluckebier, G.1    Labahn, J.2    Granzin, J.3    Saenger, W.4
  • 35
    • 0032544482 scopus 로고    scopus 로고
    • ErmE methyltransferase recognition elements in RNA substrates
    • Vester B., Nielsen A. K., Hansen L. H., Douthwaite S. ErmE methyltransferase recognition elements in RNA substrates. J. Mol. Biol. 282:1998;255-264.
    • (1998) J. Mol. Biol. , vol.282 , pp. 255-264
    • Vester, B.1    Nielsen, A.K.2    Hansen, L.H.3    Douthwaite, S.4
  • 36
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren J., Svensson L., Liljas A. Crystal structure of catechol O-methyltransferase. Nature. 368:1994;354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.2    Liljas, A.3
  • 37
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A. C., Laskowski R. A., Thornton J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 38
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum B. Erythromycin resistance by ribosome modification. Antimicrob. Agents Chemother. 39:1995;577-585.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 39
    • 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., Holzman T. F., Fesik S. W. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nature Struct. Biol. 4:1997;483-489.
    • (1997) Nature 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    Holzman, T.F.7    Fesik, S.W.8
  • 40
    • 0030767647 scopus 로고    scopus 로고
    • A theoretical examination of the factors controlling the catalytic efficiency of a transmethylation enzyme: Catechol O-methyltransferase
    • Zheng Y.-J., Bruice T. C. A theoretical examination of the factors controlling the catalytic efficiency of a transmethylation enzyme: catechol O-methyltransferase. J. Am. Chem. Soc. 119:1997;8137-8145.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8137-8145
    • Zheng, Y.-J.1    Bruice, T.C.2


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