메뉴 건너뛰기




Volumn 17, Issue 12, 2009, Pages 1649-1659

Structure and Mechanism of the Lincosamide Antibiotic Adenylyltransferase LinB

Author keywords

MICROBIO; PROTEINS

Indexed keywords

CLINDAMYCIN; NUCLEOTIDYLTRANSFERASE; PROTEIN LINB; UNCLASSIFIED DRUG;

EID: 71049134855     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.10.013     Document Type: Article
Times cited : (76)

References (49)
  • 3
    • 59849112364 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus infections
    • Bartlett J.G. Methicillin-resistant Staphylococcus aureus infections. Top. HIV Med. 16 (2008) 151-155
    • (2008) Top. HIV Med. , vol.16 , pp. 151-155
    • Bartlett, J.G.1
  • 5
    • 33644634986 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerase Beta
    • Beard W.A., and Wilson S.H. Structure and mechanism of DNA polymerase Beta. Chem. Rev. 106 (2006) 361-382
    • (2006) Chem. Rev. , vol.106 , pp. 361-382
    • Beard, W.A.1    Wilson, S.H.2
  • 7
    • 0023779532 scopus 로고
    • Inactivation of lincosaminide antibiotics in Staphylococcus. Identification of lincosaminide O-nucleotidyltransferases and comparison of the corresponding resistance genes
    • Brisson-Noel A., Delrieu P., Samain D., and Courvalin P. Inactivation of lincosaminide antibiotics in Staphylococcus. Identification of lincosaminide O-nucleotidyltransferases and comparison of the corresponding resistance genes. J. Biol. Chem. 263 (1988) 15880-15887
    • (1988) J. Biol. Chem. , vol.263 , pp. 15880-15887
    • Brisson-Noel, A.1    Delrieu, P.2    Samain, D.3    Courvalin, P.4
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 0032716399 scopus 로고    scopus 로고
    • Kinetic mechanism of kanamycin nucleotidyltransferase from Staphylococcus aureus
    • Chen-Goodspeed M., Vanhooke J.L., Holden H.M., and Raushel F.M. Kinetic mechanism of kanamycin nucleotidyltransferase from Staphylococcus aureus. Bioorg. Chem. 27 (1999) 395-408
    • (1999) Bioorg. Chem. , vol.27 , pp. 395-408
    • Chen-Goodspeed, M.1    Vanhooke, J.L.2    Holden, H.M.3    Raushel, F.M.4
  • 10
    • 0022358111 scopus 로고
    • Multiplicity of macrolide-lincosamide-streptogramin antibiotic resistance determinants
    • Courvalin P., Ounissi H., and Arthur M. Multiplicity of macrolide-lincosamide-streptogramin antibiotic resistance determinants. J. Antimicrob. Chemother. 16 Suppl A (1985) 91-100
    • (1985) J. Antimicrob. Chemother. , vol.16 , Issue.SUPPL. A , pp. 91-100
    • Courvalin, P.1    Ounissi, H.2    Arthur, M.3
  • 11
    • 0030848695 scopus 로고    scopus 로고
    • Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors
    • Daigle D.M., McKay G.A., and Wright G.D. Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors. J. Biol. Chem. 272 (1997) 24755-24758
    • (1997) J. Biol. Chem. , vol.272 , pp. 24755-24758
    • Daigle, D.M.1    McKay, G.A.2    Wright, G.D.3
  • 12
    • 0027974928 scopus 로고
    • 2.3 A crystal structure of the catalytic domain of DNA polymerase beta
    • Davies II J.F., Almassy R.J., Hostomska Z., Ferre R.A., and Hostomsky Z. 2.3 A crystal structure of the catalytic domain of DNA polymerase beta. Cell 76 (1994) 1123-1133
    • (1994) Cell , vol.76 , pp. 1123-1133
    • Davies II, J.F.1    Almassy, R.J.2    Hostomska, Z.3    Ferre, R.A.4    Hostomsky, Z.5
  • 13
    • 33646037670 scopus 로고    scopus 로고
    • An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis
    • De Leon G.P., Elowe N.H., Koteva K.P., Valvano M.A., and Wright G.D. An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis. Chem. Biol. 13 (2006) 437-441
    • (2006) Chem. Biol. , vol.13 , pp. 437-441
    • De Leon, G.P.1    Elowe, N.H.2    Koteva, K.P.3    Valvano, M.A.4    Wright, G.D.5
  • 15
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391 (1998) 251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 16
    • 0020417119 scopus 로고
    • Resistance to macrolide, lincosamide and streptogramin antibiotics and degradation of lincosamide antibiotics in streptococci from bovine mastitis
    • Dutta G.N., and Devriese L.A. Resistance to macrolide, lincosamide and streptogramin antibiotics and degradation of lincosamide antibiotics in streptococci from bovine mastitis. J. Antimicrob. Chemother. 10 (1982) 403-408
    • (1982) J. Antimicrob. Chemother. , vol.10 , pp. 403-408
    • Dutta, G.N.1    Devriese, L.A.2
  • 18
    • 0032488583 scopus 로고    scopus 로고
    • Antibiotic inhibitors of the peptidyl transferase center. 1. Clindamycin as a composite analogue of the transfer RNA fragments L-Pro-Met and the D-ribosyl ring of adenosine
    • Fitzhugh A.L. Antibiotic inhibitors of the peptidyl transferase center. 1. Clindamycin as a composite analogue of the transfer RNA fragments L-Pro-Met and the D-ribosyl ring of adenosine. Bioorg. Med. Chem. Lett. 8 (1998) 87-92
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 87-92
    • Fitzhugh, A.L.1
  • 19
    • 0024290399 scopus 로고
    • Alternative substrate and inhibition kinetics of aminoglycoside nucleotidyltransferase 2″-I in support of a Theorell-Chance kinetic mechanism
    • Gates C.A., and Northrop D.B. Alternative substrate and inhibition kinetics of aminoglycoside nucleotidyltransferase 2″-I in support of a Theorell-Chance kinetic mechanism. Biochemistry 27 (1988) 3826-3833
    • (1988) Biochemistry , vol.27 , pp. 3826-3833
    • Gates, C.A.1    Northrop, D.B.2
  • 20
    • 0035814899 scopus 로고    scopus 로고
    • Characterization of the transition-state structure of the reaction of kanamycin nucleotidyltransferase by heavy-atom kinetic isotope effects
    • Gerratana B., Frey P.A., and Cleland W.W. Characterization of the transition-state structure of the reaction of kanamycin nucleotidyltransferase by heavy-atom kinetic isotope effects. Biochemistry 40 (2001) 2972-2977
    • (2001) Biochemistry , vol.40 , pp. 2972-2977
    • Gerratana, B.1    Frey, P.A.2    Cleland, W.W.3
  • 21
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 23
    • 0029360327 scopus 로고
    • DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily
    • Holm L., and Sander C. DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily. Trends Biochem. Sci. 20 (1995) 345-347
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 345-347
    • Holm, L.1    Sander, C.2
  • 24
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm L., Kaariainen S., Rosenstrom P., and Schenkel A. Searching protein structure databases with DaliLite v.3. Bioinformatics 24 (2008) 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 25
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon W.C., McKay G.A., Thompson P.R., Sweet R.M., Yang D.S., Wright G.D., and Berghuis A.M. Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89 (1997) 887-895
    • (1997) Cell , vol.89 , pp. 887-895
    • Hon, W.C.1    McKay, G.A.2    Thompson, P.R.3    Sweet, R.M.4    Yang, D.S.5    Wright, G.D.6    Berghuis, A.M.7
  • 26
    • 55249098618 scopus 로고    scopus 로고
    • Antimicrobial agents in treatment of MRSA infections
    • Johnson M.D., and Decker C.F. Antimicrobial agents in treatment of MRSA infections. Dis. Mon. 54 (2008) 793-800
    • (2008) Dis. Mon. , vol.54 , pp. 793-800
    • Johnson, M.D.1    Decker, C.F.2
  • 27
    • 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. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0021840794 scopus 로고
    • Plasmid-mediated resistance to lincomycin by inactivation in Staphylococcus haemolyticus
    • Leclercq R., Carlier C., Duval J., and Courvalin P. Plasmid-mediated resistance to lincomycin by inactivation in Staphylococcus haemolyticus. Antimicrob. Agents Chemother. 28 (1985) 421-424
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 421-424
    • Leclercq, R.1    Carlier, C.2    Duval, J.3    Courvalin, P.4
  • 29
    • 3843067711 scopus 로고    scopus 로고
    • Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase
    • Martin G., Moglich A., Keller W., and Doublie S. Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase. J. Mol. Biol. 341 (2004) 911-925
    • (2004) J. Mol. Biol. , vol.341 , pp. 911-925
    • Martin, G.1    Moglich, A.2    Keller, W.3    Doublie, S.4
  • 30
    • 46049095239 scopus 로고    scopus 로고
    • Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein
    • Meinke G., Ezeokonkwo C., Balbo P., Stafford W., Moore C., and Bohm A. Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. Biochemistry 47 (2008) 6859-6869
    • (2008) Biochemistry , vol.47 , pp. 6859-6869
    • Meinke, G.1    Ezeokonkwo, C.2    Balbo, P.3    Stafford, W.4    Moore, C.5    Bohm, A.6
  • 31
    • 0242389785 scopus 로고    scopus 로고
    • Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure
    • Okabe M., Tomita K., Ishitani R., Ishii R., Takeuchi N., Arisaka F., Nureki O., and Yokoyama S. Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure. EMBO J. 22 (2003) 5918-5927
    • (2003) EMBO J. , vol.22 , pp. 5918-5927
    • Okabe, M.1    Tomita, K.2    Ishitani, R.3    Ishii, R.4    Takeuchi, N.5    Arisaka, F.6    Nureki, O.7    Yokoyama, S.8
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • Pedersen L.C., Benning M.M., and Holden H.M. Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34 (1995) 13305-13311
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 36
    • 34247596021 scopus 로고    scopus 로고
    • Medicinal use of lincosamides and microbial resistance to them
    • Rezanka T., Spizek J., and Sigler K. Medicinal use of lincosamides and microbial resistance to them. Anti-Infect. Agents Med. Chem. 6 (2007) 133-144
    • (2007) Anti-Infect. Agents Med. Chem. , vol.6 , pp. 133-144
    • Rezanka, T.1    Spizek, J.2    Sigler, K.3
  • 37
    • 0027496278 scopus 로고
    • Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution
    • Sakon J., Liao H.H., Kanikula A.M., Benning M.M., Rayment I., and Holden H.M. Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution. Biochemistry 32 (1993) 11977-11984
    • (1993) Biochemistry , vol.32 , pp. 11977-11984
    • Sakon, J.1    Liao, H.H.2    Kanikula, A.M.3    Benning, M.M.4    Rayment, I.5    Holden, H.M.6
  • 38
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism
    • Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., and Kraut J. Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism. Science 264 (1994) 1930-1935
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 39
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlunzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R., Yonath A., and Franceschi F. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413 (2001) 814-821
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlunzen, F.1    Zarivach, R.2    Harms, J.3    Bashan, A.4    Tocilj, A.5    Albrecht, R.6    Yonath, A.7    Franceschi, F.8
  • 40
    • 55849096934 scopus 로고    scopus 로고
    • Enterococcal infections and antimicrobial resistance
    • Sood S., Mahorta M., Das B.K., and Kapil A. Enterococcal infections and antimicrobial resistance. Indian J. Med. Res. 128 (2008) 111-121
    • (2008) Indian J. Med. Res. , vol.128 , pp. 111-121
    • Sood, S.1    Mahorta, M.2    Das, B.K.3    Kapil, A.4
  • 41
    • 9744275238 scopus 로고    scopus 로고
    • Lincosamides: chemical structure, biosynthesis, mechanism of action, resistance, and applications
    • Spizek J., Novotna J., and Rezanka T. Lincosamides: chemical structure, biosynthesis, mechanism of action, resistance, and applications. Adv. Appl. Microbiol. 56 (2004) 121-154
    • (2004) Adv. Appl. Microbiol. , vol.56 , pp. 121-154
    • Spizek, J.1    Novotna, J.2    Rezanka, T.3
  • 42
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz T.A. A mechanism for all polymerases. Nature 391 (1998) 231-232
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0037018922 scopus 로고    scopus 로고
    • Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa: role of the nucleotide positioning loop
    • Thompson P.R., Boehr D.D., Berghuis A.M., and Wright G.D. Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa: role of the nucleotide positioning loop. Biochemistry 41 (2002) 7001-7007
    • (2002) Biochemistry , vol.41 , pp. 7001-7007
    • Thompson, P.R.1    Boehr, D.D.2    Berghuis, A.M.3    Wright, G.D.4
  • 45
    • 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 P.B., and Steitz T.A. Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 121 (2005) 257-270
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 46
    • 0030561461 scopus 로고    scopus 로고
    • A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate
    • Upson R.H., Haugland R.P., and Malekzadeh M.N. A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate. Anal. Biochem. 243 (1996) 41-45
    • (1996) Anal. Biochem. , vol.243 , pp. 41-45
    • Upson, R.H.1    Haugland, R.P.2    Malekzadeh, M.N.3
  • 47
    • 0022998264 scopus 로고
    • Gentamicin nucleotidyltransferase. Stereochemical inversion at phosphorus in enzymatic 2′-deoxyadenylyl transfer to tobramycin
    • Van Pelt J.E., Iyengar R., and Frey P.A. Gentamicin nucleotidyltransferase. Stereochemical inversion at phosphorus in enzymatic 2′-deoxyadenylyl transfer to tobramycin. J. Biol. Chem. 261 (1986) 15995-15999
    • (1986) J. Biol. Chem. , vol.261 , pp. 15995-15999
    • Van Pelt, J.E.1    Iyengar, R.2    Frey, P.A.3
  • 48
    • 33847151750 scopus 로고    scopus 로고
    • The antibiotic resistome: the nexus of chemical and genetic diversity
    • Wright G.D. The antibiotic resistome: the nexus of chemical and genetic diversity. Nat. Rev. Microbiol. 5 (2007) 175-186
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 175-186
    • Wright, G.D.1
  • 49
    • 0033135707 scopus 로고    scopus 로고
    • Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold
    • Wybenga-Groot L.E., Draker K., Wright G.D., and Berghuis A.M. Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7 (1999) 497-507
    • (1999) Structure , vol.7 , pp. 497-507
    • Wybenga-Groot, L.E.1    Draker, K.2    Wright, G.D.3    Berghuis, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.