메뉴 건너뛰기




Volumn 107, Issue 40, 2010, Pages 17152-17157

Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action

Author keywords

Chloramphenicol; Clindamycin; Erythromycin; Ribosome structure; Telithromycin

Indexed keywords

ANTIBIOTIC AGENT; CHLORAMPHENICOL; CLINDAMYCIN; ERYTHROMYCIN; KETOLIDE; LINCOSAMIDE; MACROLIDE; NUCLEOTIDE; PEPTIDYLTRANSFERASE; RNA 23S; TELITHROMYCIN;

EID: 78049302075     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1007988107     Document Type: Article
Times cited : (358)

References (47)
  • 1
    • 20444498742 scopus 로고    scopus 로고
    • Antibiotic biosynthesis: Some thoughts on "why" and "how"
    • eds RA Garrett, A Liljas, AT Matheson, PB Moore, and HF Noller (ASM Press, Washington, DC)
    • Cundcliffe E (2000) Antibiotic biosynthesis: Some thoughts on "why" and "how". The Ribosome:Structure, Function, Antibiotics and Cellular Interactions, eds RA Garrett, A Liljas, AT Matheson, PB Moore, and HF Noller (ASM Press, Washington, DC), pp 409-417.
    • (2000) The Ribosome:Structure, Function, Antibiotics and Cellular Interactions , pp. 409-417
    • Cundcliffe, E.1
  • 2
    • 70349464324 scopus 로고    scopus 로고
    • SnapShot: Antibiotic inhibition of protein synthesis II
    • Sohmen D, Harms JM, Schluenzen F, Wilson DN (2009) SnapShot: Antibiotic inhibition of protein synthesis II. Cell 139 212.e211.
    • (2009) Cell , vol.139
    • Sohmen, D.1    Harms, J.M.2    Schluenzen, F.3    Wilson, D.N.4
  • 3
    • 31344478504 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase center: Structure, function, evolution, inhibition
    • Polacek N, Mankin AS (2005) The ribosomal peptidyl transferase center: Structure, function, evolution, inhibition. Crit Rev Biochem Mol Biol 40:285-311.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 285-311
    • Polacek, N.1    Mankin, A.S.2
  • 4
    • 0035160878 scopus 로고    scopus 로고
    • Macrolide resistance conferred by base substitutions in 23S rRNA
    • Vester B, Douthwaite S (2001) Macrolide resistance conferred by base substitutions in 23S rRNA. Antimicrob Agents Chemother 45:1-12.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1-12
    • Vester, B.1    Douthwaite, S.2
  • 6
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu D, Blaha G, Moore PB, Steitz TA (2005) Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 121:257-270.
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 7
    • 28144441826 scopus 로고    scopus 로고
    • The bacterial ribosome as a target for antibiotics
    • Poehlsgaard J, Douthwaite S (2005) The bacterial ribosome as a target for antibiotics. Nat Rev Microbiol 3:870-881.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 870-881
    • Poehlsgaard, J.1    Douthwaite, S.2
  • 8
    • 0021888455 scopus 로고
    • Chloramphenicol-erythromycin resistance mutations in a 23S rRNA gene of Escherichia coli
    • Ettayebi M, Prasad SM, Morgan EA (1985) Chloramphenicol-erythromycin resistance mutations in a 23S rRNA gene of Escherichia coli. J Bacteriol 162:551-557.
    • (1985) J Bacteriol , vol.162 , pp. 551-557
    • Ettayebi, M.1    Prasad, S.M.2    Morgan, E.A.3
  • 9
    • 0036137010 scopus 로고    scopus 로고
    • Diversity of ribosomal mutations conferring resistance to macrolides, clindamycin, streptogramin, and telithromycin in Streptococcus pneumoniae
    • Canu A, et al. (2002) Diversity of ribosomal mutations conferring resistance to macrolides, clindamycin, streptogramin, and telithromycin in Streptococcus pneumoniae. Antimicrob Agents Chemother 46:125-131.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 125-131
    • Canu, A.1
  • 10
    • 0025892855 scopus 로고
    • Chloramphenicol resistance mutations in the single 23S ribosomal RNA gene of the archaeon Halobacterium halobium
    • Mankin AS, Garrett RA (1991) Chloramphenicol resistance mutations in the single 23S ribosomal RNA gene of the archaeon Halobacterium halobium. J Bacteriol 173:3559-3563.
    • (1991) J Bacteriol , vol.173 , pp. 3559-3563
    • Mankin, A.S.1    Garrett, R.A.2
  • 11
    • 29044436081 scopus 로고    scopus 로고
    • Species-specific antibiotic-ribosome interactions: Implications for drug development
    • Wilson DN, Harms JM, Nierhaus KH, Schlunzen F, Fucini P (2005) Species-specific antibiotic-ribosome interactions: Implications for drug development. Biol Chem 386:1239-1252.
    • (2005) Biol Chem , vol.386 , pp. 1239-1252
    • Wilson, D.N.1    Harms, J.M.2    Nierhaus, K.H.3    Schlunzen, F.4    Fucini, P.5
  • 12
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schluenzen F, et al. (2001) Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413:814-821.
    • (2001) Nature , vol.413 , pp. 814-821
    • Schluenzen, F.1
  • 13
    • 0038492422 scopus 로고    scopus 로고
    • Structural insight into the antibiotic action of telithromycin against resistant mutants
    • Berisio R, et al. (2003) Structural insight into the antibiotic action of telithromycin against resistant mutants. J Bacteriol 185:4276-4279.
    • (2003) J Bacteriol , vol.185 , pp. 4276-4279
    • Berisio, R.1
  • 14
    • 0036342198 scopus 로고    scopus 로고
    • The structures of four macrolide antibiotics bound to the large ribosomal subunit
    • Hansen JL, et al. (2002) The structures of four macrolide antibiotics bound to the large ribosomal subunit. Mol Cell 10:117-128.
    • (2002) Mol Cell , vol.10 , pp. 117-128
    • Hansen, J.L.1
  • 15
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen JL, Moore PB, Steitz TA (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol 330:1061-1075.
    • (2003) J Mol Biol , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 16
    • 0030722151 scopus 로고    scopus 로고
    • Solid-state investigations of erythromycin A dihydrate: Structure, NMR spectroscopy, and hygroscopicity
    • Stephenson G, Stowell J, Toma P, Pfeiffer R, Byrn S (1997) Solid-state investigations of erythromycin A dihydrate: Structure, NMR spectroscopy, and hygroscopicity. J Pharm Sci 86:1239-1244.
    • (1997) J Pharm Sci , vol.86 , pp. 1239-1244
    • Stephenson, G.1    Stowell, J.2    Toma, P.3    Pfeiffer, R.4    Byrn, S.5
  • 17
    • 43049089746 scopus 로고    scopus 로고
    • Molecular mechanism of drugdependent ribosome stalling
    • Vazquez-Laslop N, Thum C, Mankin AS (2008) Molecular mechanism of drugdependent ribosome stalling. Mol Cell 30:190-202.
    • (2008) Mol Cell , vol.30 , pp. 190-202
    • Vazquez-Laslop, N.1    Thum, C.2    Mankin, A.S.3
  • 18
    • 0032950956 scopus 로고    scopus 로고
    • The macrolide-ketolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA
    • Hansen LH, Mauvais P, Douthwaite S (1999) The macrolide-ketolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA. Mol Microbiol 31:623-631.
    • (1999) Mol Microbiol , vol.31 , pp. 623-631
    • Hansen, L.H.1    Mauvais, P.2    Douthwaite, S.3
  • 19
    • 0032904341 scopus 로고    scopus 로고
    • A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre
    • Xiong L, Shah S, Mauvais P, Mankin AS (1999) A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre. Mol Microbiol 31:633-639.
    • (1999) Mol Microbiol , vol.31 , pp. 633-639
    • Xiong, L.1    Shah, S.2    Mauvais, P.3    Mankin, A.S.4
  • 20
    • 0035162904 scopus 로고    scopus 로고
    • Binding site of macrolide antibiotics on the ribosome: New resistance mutation identifies a specific interaction of ketolides with rRNA
    • Garza-Ramos G, Xiong L, Zhong P, Mankin A (2001) Binding site of macrolide antibiotics on the ribosome: New resistance mutation identifies a specific interaction of ketolides with rRNA. J Bacteriol 183:6898-6907.
    • (2001) J Bacteriol , vol.183 , pp. 6898-6907
    • Garza-Ramos, G.1    Xiong, L.2    Zhong, P.3    Mankin, A.4
  • 21
    • 11244307407 scopus 로고    scopus 로고
    • Binding site of the bridged macrolides in the Escherichia coli ribosome
    • Xiong L, Korkhin Y, Mankin AS (2005) Binding site of the bridged macrolides in the Escherichia coli ribosome. Antimicrob Agents Chemother 49:281-288.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 281-288
    • Xiong, L.1    Korkhin, Y.2    Mankin, A.S.3
  • 23
    • 66149157000 scopus 로고    scopus 로고
    • Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
    • Voorhees RM, Weixlbaumer A, Loakes D, Kelley AC, Ramakrishnan V (2009) Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nat Struct Mol Biol 16:528-533.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 528-533
    • Voorhees, R.M.1    Weixlbaumer, A.2    Loakes, D.3    Kelley, A.C.4    Ramakrishnan, V.5
  • 24
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen JL, Moore PB, Steitz TA (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol 330:1061-1075.
    • (2003) J Mol Biol , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 25
    • 0015831640 scopus 로고
    • Identification of the chloramphenicol-binding protein in Escherichia coli ribosomes by partial reconstitution
    • Nierhaus D, Nierhaus KH (1973) Identification of the chloramphenicol- binding protein in Escherichia coli ribosomes by partial reconstitution. Proc Natl Acad Sci USA 70:2224-2228.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2224-2228
    • Nierhaus, D.1    Nierhaus, K.H.2
  • 26
    • 43449093704 scopus 로고    scopus 로고
    • Mutations outside the anisomycin-binding site can make ribosomes drug-resistant
    • Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA (2008) Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J Mol Biol 379:505-519.
    • (2008) J Mol Biol , vol.379 , pp. 505-519
    • Blaha, G.1    Gurel, G.2    Schroeder, S.J.3    Moore, P.B.4    Steitz, T.A.5
  • 27
    • 0023139432 scopus 로고
    • 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80S ribosome targeted antibiotic anisomycin
    • Hummel H, Böck A (1987) 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80S ribosome targeted antibiotic anisomycin. Nucleic Acids Res 15:2431-2443.
    • (1987) Nucleic Acids Res , vol.15 , pp. 2431-2443
    • Hummel, H.1    Böck, A.2
  • 28
    • 2942571539 scopus 로고    scopus 로고
    • The comparative RNA web (CRW) site: An online database of comparative sequence and structure information for ribosomal, intron, and other RNAs
    • Cannone JJ, et al. (2002) The comparative RNA web (CRW) site: An online database of comparative sequence and structure information for ribosomal, intron, and other RNAs. BMC Bioinformatics 3:2.
    • (2002) BMC Bioinformatics , vol.3 , pp. 2
    • Cannone, J.J.1
  • 29
    • 34248326491 scopus 로고    scopus 로고
    • Induced-fit tightens pleuromutilins binding to ribosomes and remote interactions enable their selectivity
    • Davidovich C, et al. (2007) Induced-fit tightens pleuromutilins binding to ribosomes and remote interactions enable their selectivity. Proc Natl Acad Sci USA 104:4291-4296.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4291-4296
    • Davidovich, C.1
  • 30
    • 67349260439 scopus 로고    scopus 로고
    • U2504 determines the species specificity of the A-site cleft antibiotics: The structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome
    • Gürel G, Blaha G, Moore PB, Steitz TA (2009) U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome. J Mol Biol 389:146-156.
    • (2009) J Mol Biol , vol.389 , pp. 146-156
    • Gürel, G.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 31
    • 60649086618 scopus 로고    scopus 로고
    • Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket
    • Long KS, et al. (2009) Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket. Mol Microbiology 71:1218-1227.
    • (2009) Mol Microbiology , vol.71 , pp. 1218-1227
    • Long, K.S.1
  • 32
    • 9644281855 scopus 로고    scopus 로고
    • Inhibition of peptide bond formation by pleuromutilins: The structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin
    • Schlünzen F, Pyetan E, Fucini P, Yonath A, Harms JM (2004) Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin. Mol Microbiol 54:1287-1294.
    • (2004) Mol Microbiol , vol.54 , pp. 1287-1294
    • Schlünzen, F.1    Pyetan, E.2    Fucini, P.3    Yonath, A.4    Harms, J.M.5
  • 33
    • 0040843291 scopus 로고
    • Mitochondrial DNA of chloramphenicol resistant mouse cells contains a single nucleotide change in the region encoding the 3′ end of the large ribosomal RNA
    • Blanc H, Wright CT, Bibb MJ, Wallace DC, Clayton DA (1981) Mitochondrial DNA of chloramphenicol resistant mouse cells contains a single nucleotide change in the region encoding the 3′ end of the large ribosomal RNA. Proc Natl Acad Sci USA 78:3789-3793.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3789-3793
    • Blanc, H.1    Wright, C.T.2    Bibb, M.J.3    Wallace, D.C.4    Clayton, D.A.5
  • 34
    • 45649083395 scopus 로고    scopus 로고
    • An indigenous posttranscriptional modification in the ribosomal peptidyl transferase center confers resistance to an array of protein synthesis inhibitors
    • Toh SM, Mankin AS (2008) An indigenous posttranscriptional modification in the ribosomal peptidyl transferase center confers resistance to an array of protein synthesis inhibitors. J Mol Biol 380:593-597.
    • (2008) J Mol Biol , vol.380 , pp. 593-597
    • Toh, S.M.1    Mankin, A.S.2
  • 35
  • 36
    • 40449123425 scopus 로고    scopus 로고
    • Mutation from guanine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae
    • Bommakanti AS, Lindahl L, Zengel JM (2008) Mutation from guanine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae. RNA 14:460-464.
    • (2008) RNA , vol.14 , pp. 460-464
    • Bommakanti, A.S.1    Lindahl, L.2    Zengel, J.M.3
  • 37
    • 27644491082 scopus 로고    scopus 로고
    • Structures of the bacterial ribosome at 3.5 A resolution
    • Schuwirth BS, et al. (2005) Structures of the bacterial ribosome at 3.5 A resolution. Science 310:827-834.
    • (2005) Science , vol.310 , pp. 827-834
    • Schuwirth, B.S.1
  • 38
    • 69249112231 scopus 로고    scopus 로고
    • Structures of the ribosome in intermediate states of ratcheting
    • Zhang W, Dunkle JA, Cate JH (2009) Structures of the ribosome in intermediate states of ratcheting. Science 325:1014-1017.
    • (2009) Science , vol.325 , pp. 1014-1017
    • Zhang, W.1    Dunkle, J.A.2    Cate, J.H.3
  • 39
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D 66:213-221.
    • (2010) Acta Crystallogr D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 43
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites
    • Moazed D, Noller HF (1989) Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites. Cell 57:585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 44
    • 0026721044 scopus 로고
    • Introducing mutations into the single-copy chromosomal 23S rRNA gene of the archaeon Halobacterium halobium by using an rRNA operon-based transformation system
    • Mankin AS, Zyrianova IM, Kagramanova VK, Garrett RA (1992) Introducing mutations into the single-copy chromosomal 23S rRNA gene of the archaeon Halobacterium halobium by using an rRNA operon-based transformation system. Proc Natl Acad Sci USA 89:6535-6539.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6535-6539
    • Mankin, A.S.1    Zyrianova, I.M.2    Kagramanova, V.K.3    Garrett, R.A.4
  • 45
    • 0030590258 scopus 로고    scopus 로고
    • Mutations in the peptidyl transferase center of 23S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation
    • Tan GT, DeBlasio A, Mankin AS (1996) Mutations in the peptidyl transferase center of 23S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation. J Mol Biol 261:222-230.
    • (1996) J Mol Biol , vol.261 , pp. 222-230
    • Tan, G.T.1    DeBlasio, A.2    Mankin, A.S.3
  • 46
    • 0003098935 scopus 로고    scopus 로고
    • Footprinting and modification-interference analysis of binding sites on RNA
    • ed CWJ Smith (Oxford University Press, Oxford)
    • Merryman C, Noller HF (1998) Footprinting and modification-interference analysis of binding sites on RNA. RNA:Protein Interactions, A Practical Approach, ed CWJ Smith (Oxford University Press, Oxford).
    • (1998) RNA:Protein Interactions, a Practical Approach
    • Merryman, C.1    Noller, H.F.2
  • 47
    • 0030660210 scopus 로고    scopus 로고
    • Pactamycin resistance mutations in functional sites of 16S rRNA
    • Mankin AS (1997) Pactamycin resistance mutations in functional sites of 16S rRNA. J Mol Biol 274:8-15.
    • (1997) J Mol Biol , vol.274 , pp. 8-15
    • Mankin, A.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.