메뉴 건너뛰기




Volumn 107, Issue 5, 2010, Pages 1983-1988

The structure of ribosome-lankacidin complex reveals ribosomal sites for synergistic antibiotics

Author keywords

Lankamycin; Resistance; Ribosomes; rRNA; Synergism

Indexed keywords

DALFOPRISTIN; ERYTHROMYCIN; LANKACIDIN C; LANKACIDIN M; LANKAMYCIN; PEPTIDYLTRANSFERASE; QUINUPRISTIN; STREPTOGRAMIN DERIVATIVE; UNCLASSIFIED DRUG; VIRGINIAMYCIN M; VIRGINIAMYCIN S;

EID: 76649088360     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0914100107     Document Type: Article
Times cited : (59)

References (66)
  • 1
    • 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(11):870-881.
    • (2005) Nat Rev Microbiol , vol.3 , Issue.11 , pp. 870-881
    • Poehlsgaard, J.1    Douthwaite, S.2
  • 2
    • 33646109801 scopus 로고    scopus 로고
    • The ribosome as a drug target
    • Bottger EC (2006) The ribosome as a drug target. Trends Biotechnol, 24(4):145-147.
    • (2006) Trends Biotechnol , vol.24 , Issue.4 , pp. 145-147
    • Bottger, E.C.1
  • 3
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase center in eubacteria
    • Schluenzen F, et al. (2001) Structural basis for the interaction of antibiotics with the peptidyl transferase center in eubacteria. Nature, 413(6858):814-821.
    • (2001) Nature , vol.413 , Issue.6858 , pp. 814-821
    • Schluenzen, F.1
  • 4
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen JL, et al. (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol, 330(5):1061-1075.
    • (2003) J Mol Biol , vol.330 , Issue.5 , pp. 1061-1075
    • Hansen, J.L.1
  • 5
    • 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
    • Schluenzen F, et al. (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(5):1287-1294.
    • (2004) Mol Microbiol , vol.54 , Issue.5 , pp. 1287-1294
    • Schluenzen, F.1
  • 6
    • 3242712966 scopus 로고    scopus 로고
    • Harms J, et al. (2004) Alterations at the peptidyl transferase center of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin. BMC Biol, 2(1):4;1-10.
    • Harms J, et al. (2004) Alterations at the peptidyl transferase center of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin. BMC Biol, 2(1):4;1-10.
  • 7
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu D, et al. (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
  • 8
    • 34247562698 scopus 로고    scopus 로고
    • The site of action of oxazolidinone antibiotics in living bacteria and in human mitochondria
    • Leach KL, et al. (2007) The site of action of oxazolidinone antibiotics in living bacteria and in human mitochondria. Mol Cell, 26(3):393-402.
    • (2007) Mol Cell , vol.26 , Issue.3 , pp. 393-402
    • Leach, K.L.1
  • 9
    • 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 (11):4291-4296.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.11 , pp. 4291-4296
    • Davidovich, C.1
  • 10
    • 58549118714 scopus 로고    scopus 로고
    • Structural basis for cross-resistance to ribosomal PTC antibiotics
    • Davidovich C, et al. (2008) Structural basis for cross-resistance to ribosomal PTC antibiotics. Proc Natl Acad Sci USA, 105(52):20665-20670.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.52 , pp. 20665-20670
    • Davidovich, C.1
  • 11
    • 45749089015 scopus 로고    scopus 로고
    • Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit
    • Ippolito JA, et al. (2008) Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit. J Med Chem, 51(12):3353-3356.
    • (2008) J Med Chem , vol.51 , Issue.12 , pp. 3353-3356
    • Ippolito, J.A.1
  • 12
    • 51649117099 scopus 로고    scopus 로고
    • The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning
    • Wilson DN, et al. (2008) The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning. Proc Natl Acad Sci USA, 105(26):13339-13344.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.26 , pp. 13339-13344
    • Wilson, D.N.1
  • 13
    • 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
    • Gurel G, et al. (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(1):146-156.
    • (2009) J Mol Biol , vol.389 , Issue.1 , pp. 146-156
    • Gurel, G.1
  • 14
    • 62949208876 scopus 로고    scopus 로고
    • Structural basis for the antibacterial activity of the 12-membered-ring mono-sugar macrolide methymycin
    • Auerbach T, et al. (2009) Structural basis for the antibacterial activity of the 12-membered-ring mono-sugar macrolide methymycin. Biotechnolog, 84:24-35.
    • (2009) Biotechnolog , vol.84 , pp. 24-35
    • Auerbach, T.1
  • 15
    • 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(5):285-311.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , Issue.5 , pp. 285-311
    • Polacek, N.1    Mankin, A.S.2
  • 16
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA
    • Moazed D, Noller HF (1987) Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie, 69:879-884.
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 17
    • 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 center
    • Xiong L, et al. (1999) A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase center. Mol Microbiol, 31(2):633-639.
    • (1999) Mol Microbiol , vol.31 , Issue.2 , pp. 633-639
    • Xiong, L.1
  • 18
    • 0037334850 scopus 로고    scopus 로고
    • Structural basis for the antibiotic activity of ketolides and azalides
    • Schluenzen F, et al. (2003) Structural basis for the antibiotic activity of ketolides and azalides. Structure, 11(3):329-338.
    • (2003) Structure , vol.11 , Issue.3 , pp. 329-338
    • Schluenzen, F.1
  • 19
    • 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(14):4276-4279.
    • (2003) J Bacteriol , vol.185 , Issue.14 , pp. 4276-4279
    • Berisio, R.1
  • 20
    • 0037407668 scopus 로고    scopus 로고
    • Structural insight into the role of the ribosomal tunnel in cellular regulation
    • Berisio R, et al. (2003) Structural insight into the role of the ribosomal tunnel in cellular regulation. Nat Struct Biol, 10(5):366-370.
    • (2003) Nat Struct Biol , vol.10 , Issue.5 , pp. 366-370
    • Berisio, R.1
  • 21
    • 0037069328 scopus 로고    scopus 로고
    • Resistance to the macrolide antibiotic tylosin is conferred by single methylations at 23S rRNA nucleotides G748 and A2058 acting in synergy
    • Liu M, Douthwaite S (2002) Resistance to the macrolide antibiotic tylosin is conferred by single methylations at 23S rRNA nucleotides G748 and A2058 acting in synergy. Proc Natl Acad Sci USA, 99(23):14658-14663.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.23 , pp. 14658-14663
    • Liu, M.1    Douthwaite, S.2
  • 22
    • 0033658368 scopus 로고    scopus 로고
    • Antibiotic synergy and antagonism
    • Acar JF (2000) Antibiotic synergy and antagonism. Med Clin N Am, 84(6):1391-1406.
    • (2000) Med Clin N Am , vol.84 , Issue.6 , pp. 1391-1406
    • Acar, J.F.1
  • 23
    • 76649083053 scopus 로고    scopus 로고
    • Vazquez D () Mechanism of action of antimicrobial and antitumor agents. In Antibiotics III, ed Corcoran JW(1975) (Springer-Verlag), pp 521-534.
    • Vazquez D () Mechanism of action of antimicrobial and antitumor agents. In Antibiotics III, ed Corcoran JW(1975) (Springer-Verlag), pp 521-534.
  • 24
    • 0030983411 scopus 로고    scopus 로고
    • Inhibition of protein synthesis by streptogramins and related antibiotics
    • Cocito C, et al. (1997) Inhibition of protein synthesis by streptogramins and related antibiotics. J Antimicrob Chemother, 39(Suppl A):7-13.
    • (1997) J Antimicrob Chemother , vol.39 , Issue.SUPPL. A , pp. 7-13
    • Cocito, C.1
  • 25
    • 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(1):125-131.
    • (2002) Antimicrob Agents Chemother , vol.46 , Issue.1 , pp. 125-131
    • Canu, A.1
  • 26
    • 0033673271 scopus 로고    scopus 로고
    • Quinupristin-dalfopristin: An overview
    • Delgado G, Jr, et al. (2000) Quinupristin-dalfopristin: An overview. Pharmacotherapy, 20(12):1469-1485.
    • (2000) Pharmacotherapy , vol.20 , Issue.12 , pp. 1469-1485
    • Delgado Jr, G.1
  • 27
    • 84981837496 scopus 로고
    • Stoffwechselprodukte von Actinomyceten. 21. Mitteilung. Lankamycin und Lankacidin
    • Gaumann E, et al. (1960) Stoffwechselprodukte von Actinomyceten. 21. Mitteilung. Lankamycin und Lankacidin. Helv Chim Acta, 43(2):601-606.
    • (1960) Helv Chim Acta , vol.43 , Issue.2 , pp. 601-606
    • Gaumann, E.1
  • 28
    • 0028587692 scopus 로고
    • Isolation and characterization of linear plasmids from lankacidin-producing Streptomyces species
    • Kinashi H, et al. (1994) Isolation and characterization of linear plasmids from lankacidin-producing Streptomyces species. J Antibiot, 47(12):1447-1455.
    • (1994) J Antibiot , vol.47 , Issue.12 , pp. 1447-1455
    • Kinashi, H.1
  • 29
    • 0014525915 scopus 로고
    • The structures of Bundlin A (lankacidin) and Bundlin B
    • Uramoto M, et al. (1969) The structures of Bundlin A (lankacidin) and Bundlin B. Tetrahedron Lett, 27:2249-2254.
    • (1969) Tetrahedron Lett , vol.27 , pp. 2249-2254
    • Uramoto, M.1
  • 30
    • 0014528456 scopus 로고
    • Isolation and structures of T-2636 antibiotics
    • Harada S, et al. (1969) Isolation and structures of T-2636 antibiotics. Tetrahedron Lett, 27:2239-2244.
    • (1969) Tetrahedron Lett , vol.27 , pp. 2239-2244
    • Harada, S.1
  • 31
    • 0015895971 scopus 로고
    • Studies on lankacidin-group (T-2636) antibiotics. VII. Structureactivity relationships of lankacidin-group antibiotics
    • Harada S, et al. (1973) Studies on lankacidin-group (T-2636) antibiotics. VII. Structureactivity relationships of lankacidin-group antibiotics. J Antibiot, 26(11):647-657.
    • (1973) J Antibiot , vol.26 , Issue.11 , pp. 647-657
    • Harada, S.1
  • 33
    • 0021363357 scopus 로고
    • Side chain modifications in lankacidin group antibiotics
    • McFarland JW, et al. (1984) Side chain modifications in lankacidin group antibiotics. Antimicrob Agents Chemother, 25(2):226-233.
    • (1984) Antimicrob Agents Chemother , vol.25 , Issue.2 , pp. 226-233
    • McFarland, J.W.1
  • 34
    • 0038644393 scopus 로고    scopus 로고
    • The large linear plasmid pSLA2-L of Streptomyces rochei has an unusually condensed gene organization for secondary metabolism
    • Mochizuki S, et al. (2003) The large linear plasmid pSLA2-L of Streptomyces rochei has an unusually condensed gene organization for secondary metabolism. Mol Microbiol, 48(6):1501-1510.
    • (2003) Mol Microbiol , vol.48 , Issue.6 , pp. 1501-1510
    • Mochizuki, S.1
  • 35
    • 0016744505 scopus 로고
    • Antitumor and immunosuppressive activities of lankacidin-group antibiotics: Structure-activity relationships
    • Oostu K, et al. (1975) Antitumor and immunosuppressive activities of lankacidin-group antibiotics: Structure-activity relationships. Cancer Chemother Rep, 59(5):919-928.
    • (1975) Cancer Chemother Rep , vol.59 , Issue.5 , pp. 919-928
    • Oostu, K.1
  • 36
    • 0017068249 scopus 로고
    • 3′-de-o-methyl-2′, 3′-anhydro-lankamycin, a new macrolide antibiotic from Streptomyces violaceoniger
    • Martin JR, et al. (1976) 3′-de-o-methyl-2′, 3′-anhydro-lankamycin, a new macrolide antibiotic from Streptomyces violaceoniger. Helv Chim Acta, 59(5):1886-1894.
    • (1976) Helv Chim Acta , vol.59 , Issue.5 , pp. 1886-1894
    • Martin, J.R.1
  • 37
    • 0014582958 scopus 로고    scopus 로고
    • Omura S, et al. (1969) Studies on the antibiotics from Streptomyces spinichromogenes var. kujimyceticus. II. Isolation and characterization of kujimycins A and B. J Antibiot, 22(10):500-505.
    • Omura S, et al. (1969) Studies on the antibiotics from Streptomyces spinichromogenes var. kujimyceticus. II. Isolation and characterization of kujimycins A and B. J Antibiot, 22(10):500-505.
  • 38
    • 0002226377 scopus 로고    scopus 로고
    • Macrolides: Structures and microbial targets
    • Retsema J, Fu W (2001) Macrolides: Structures and microbial targets. Int J Antimicrob Ag, 18(Suppl 1):3-10.
    • (2001) Int J Antimicrob Ag , vol.18 , Issue.SUPPL. 1 , pp. 3-10
    • Retsema, J.1    Fu, W.2
  • 39
    • 34250755407 scopus 로고
    • gamma-Butyrolactone autoregulator-receptor system involved in lankacidin and lankamycin production and morphological differentiation in Streptomyces rochei
    • 2007
    • Arakawa K, et al. (2007) gamma-Butyrolactone autoregulator-receptor system involved in lankacidin and lankamycin production and morphological differentiation in Streptomyces rochei. Microbiology+, 153(Pt 6):1817-1827.
    • (1817) Microbiology , Issue.PART 6 , pp. 153
    • Arakawa, K.1
  • 40
    • 38949186517 scopus 로고    scopus 로고
    • Gamma-butyrolactone-dependent expression of the Streptomyces antibiotic regulatory protein gene srrY plays a central role in the regulatory cascade leading to lankacidin and lankamycin production in Streptomyces rochei
    • Yamamoto S, et al. (2008) Gamma-butyrolactone-dependent expression of the Streptomyces antibiotic regulatory protein gene srrY plays a central role in the regulatory cascade leading to lankacidin and lankamycin production in Streptomyces rochei. J Bacteriol, 190(4):1308-1316.
    • (2008) J Bacteriol , vol.190 , Issue.4 , pp. 1308-1316
    • Yamamoto, S.1
  • 41
    • 0035977093 scopus 로고    scopus 로고
    • High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
    • Harms J, et al. (2001) High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. Cell, 107(5):679-688.
    • (2001) Cell , vol.107 , Issue.5 , pp. 679-688
    • Harms, J.1
  • 42
    • 0014527575 scopus 로고
    • x-ray analysis of an antibiotic, T-2636 A (Bundlin B)
    • Kamiya K, et al. (1969) x-ray analysis of an antibiotic, T-2636 A (Bundlin B). Tetrahedron Lett, 27:2245-2248.
    • (1969) Tetrahedron Lett , vol.27 , pp. 2245-2248
    • Kamiya, K.1
  • 43
    • 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(1):117-128.
    • (2002) Mol Cell , vol.10 , Issue.1 , pp. 117-128
    • Hansen, J.L.1
  • 44
    • 0037249473 scopus 로고    scopus 로고
    • Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
    • Bashan A, et al. (2003) Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression. Mol Cell, 11:91-102.
    • (2003) Mol Cell , vol.11 , pp. 91-102
    • Bashan, A.1
  • 45
    • 2542445275 scopus 로고    scopus 로고
    • Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
    • Agmon I, et al. (2004) Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. FEBS Lett, 567(1):20-26.
    • (2004) FEBS Lett , vol.567 , Issue.1 , pp. 20-26
    • Agmon, I.1
  • 46
    • 0003098935 scopus 로고    scopus 로고
    • Footprinting and modification-interference analysis of binding sites on RNA
    • ed Smith CWJ Oxford Univ Press, UK, pp
    • Merryman C, Noller HF (1998) Footprinting and modification-interference analysis of binding sites on RNA. RNA:Protein Interactions, ed Smith CWJ (Oxford Univ Press, UK), pp 237-253.
    • (1998) RNA:Protein Interactions , pp. 237-253
    • Merryman, C.1    Noller, H.F.2
  • 48
    • 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(4):585-597.
    • (1989) Cell , vol.57 , Issue.4 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 49
    • 8344271978 scopus 로고    scopus 로고
    • Functional aspects of ribosomal architecture: Symmetry, chirality and regulation
    • Zarivach R, et al. (2004) Functional aspects of ribosomal architecture: Symmetry, chirality and regulation. J Phys Org Chem, 17:901-912.
    • (2004) J Phys Org Chem , vol.17 , pp. 901-912
    • Zarivach, R.1
  • 50
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing TM, et al. (2005) An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature, 438(7067):520-524.
    • (2005) Nature , vol.438 , Issue.7067 , pp. 520-524
    • Schmeing, T.M.1
  • 51
    • 0033582599 scopus 로고    scopus 로고
    • Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms
    • Porse BT, Garrett RA (1999) Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms. J Mol Biol, 286(2):375-387.
    • (1999) J Mol Biol , vol.286 , Issue.2 , pp. 375-387
    • Porse, B.T.1    Garrett, R.A.2
  • 52
    • 0035173131 scopus 로고    scopus 로고
    • Recent developments on ketolides and macrolides
    • Wu YJ, Su WG (2001) Recent developments on ketolides and macrolides. Curr Med Chem, 8(14):1727-1758.
    • (2001) Curr Med Chem , vol.8 , Issue.14 , pp. 1727-1758
    • Wu, Y.J.1    Su, W.G.2
  • 53
    • 22244433549 scopus 로고    scopus 로고
    • Antibiotics targeting ribosomes: Resistance, selectivity, synergism, and cellular regulation
    • Yonath A (2005) Antibiotics targeting ribosomes: Resistance, selectivity, synergism, and cellular regulation. Annu Rev Biochem, 74:649-679.
    • (2005) Annu Rev Biochem , vol.74 , pp. 649-679
    • Yonath, A.1
  • 54
    • 43049089746 scopus 로고    scopus 로고
    • Molecular mechanism of drug-dependent ribosome stalling
    • Vazquez-Laslop N, et al. (2008) Molecular mechanism of drug-dependent ribosome stalling. Mol Cell, 30(2):190-202.
    • (2008) Mol Cell , vol.30 , Issue.2 , pp. 190-202
    • Vazquez-Laslop, N.1
  • 55
    • 17044425907 scopus 로고    scopus 로고
    • 23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A-> G
    • Pfister P, et al. (2005) 23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A-> G. Proc Natl Acad Sci USA, 102(14):5180-5185.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.14 , pp. 5180-5185
    • Pfister, P.1
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode, methods in enzymology
    • ed Carter JCW pp
    • Otwinowski Z, Minor W (1997) Processing of x-ray diffraction data collected in oscillation mode, methods in enzymology. Macromolecular Crystallography, , ed Carter JCW pp:307-326.
    • (1997) Macromolecular Crystallography , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 76649097138 scopus 로고    scopus 로고
    • CCP4 (1994) Collaborative Computational Project, Number 4, The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr D, pp:760-763.
    • CCP4 (1994) Collaborative Computational Project, Number 4, The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr D, pp:760-763.
  • 58
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D, 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 59
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D, 54(Pt 5):905-921.
    • (1998) Acta Crystallogr D , vol.54 , Issue.PART 5 , pp. 905-921
    • Brunger, A.T.1
  • 60
    • 37049014272 scopus 로고    scopus 로고
    • The crystallography and NMR system
    • Brunger AT (2007) The crystallography and NMR system. Nat Protoc, 2(11):2728-2733.
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 61
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, et al. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng, 8(2):127-134.
    • (1995) Protein Eng , vol.8 , Issue.2 , pp. 127-134
    • Wallace, A.C.1
  • 62
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • Sobolev V, et al. (1999) Automated analysis of interatomic contacts in proteins. Bioinformatics, 15(4):327-332.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 327-332
    • Sobolev, V.1
  • 64
    • 11244307407 scopus 로고    scopus 로고
    • Binding Site of the Bridged Macrolides in the Escherichia coli Ribosome
    • Xiong L, et al. (2005) Binding Site of the Bridged Macrolides in the Escherichia coli Ribosome. Antimicrob Agents Chemother, 49(1):281-288.
    • (2005) Antimicrob Agents Chemother , vol.49 , Issue.1 , pp. 281-288
    • Xiong, L.1
  • 65
    • 27644598282 scopus 로고    scopus 로고
    • A protein component at the heart of an RNA machine: The importance of protein L27 for the function of the bacterial ribosome
    • Maguire BA, et al. (2005) A protein component at the heart of an RNA machine: the importance of protein L27 for the function of the bacterial ribosome. Mol Cell, 20(3):427-436.
    • (2005) Mol Cell , vol.20 , Issue.3 , pp. 427-436
    • Maguire, B.A.1
  • 66
    • 0024166218 scopus 로고
    • Mg2 + /NH4 + /polyamine system for polyuridinedependent polyphenylalanine synthesis with near in vivo characteristics
    • Bartetzko A, Nierhaus KH (1988) Mg2 + /NH4 + /polyamine system for polyuridinedependent polyphenylalanine synthesis with near in vivo characteristics. Methods Enzymol, 164:650-658.
    • (1988) Methods Enzymol , vol.164 , pp. 650-658
    • Bartetzko, A.1    Nierhaus, K.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.