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Volumn 7, Issue , 2016, Pages

Rifampin phosphotransferase is an unusual antibiotic resistance kinase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PHOSPHOTRANSFERASE; RIFAMPICIN; ADENOSINE TRIPHOSPHATE; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84971669517     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11343     Document Type: Article
Times cited : (39)

References (58)
  • 1
    • 84969206734 scopus 로고    scopus 로고
    • Solving the antibiotic crisis
    • Wright, G. D. Solving the antibiotic crisis. ACS Infect. Dis. 2, 80-84
    • ACS Infect. Dis. , vol.2 , pp. 80-84
    • Wright, G.D.1
  • 2
    • 0242711908 scopus 로고
    • Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria
    • Benveniste, R., & Davies, J. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc. Natl Acad. Sci. USA 70, 2276-2280 (1973).
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 2276-2280
    • Benveniste, R.1    Davies, J.2
  • 3
    • 84865531061 scopus 로고    scopus 로고
    • The shared antibiotic resistome of soil bacteria and human pathogens
    • Forsberg, K. J., et al. The shared antibiotic resistome of soil bacteria and human pathogens. Science 337, 1107-1111 (2012).
    • (2012) Science , vol.337 , pp. 1107-1111
    • Forsberg, K.J.1
  • 4
    • 0030911603 scopus 로고    scopus 로고
    • D Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB
    • Marshall, C. G., Broadhead, G., Leskiw, B. K., & Wright, G. D. D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB. Proc. Natl Acad. Sci. USA 94, 6480-6483 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6480-6483
    • Marshall, C.G.1    Broadhead, G.2    Leskiw, B.K.3    Wright, G.D.4
  • 5
    • 80053130409 scopus 로고    scopus 로고
    • Antibiotic resistance is ancient
    • D'Costa, V. M., et al. Antibiotic resistance is ancient. Nature 477, 457-461 (2011).
    • (2011) Nature , vol.477 , pp. 457-461
    • D'Costa, V.M.1
  • 7
    • 84859574738 scopus 로고    scopus 로고
    • Antibiotic resistance is prevalent in an isolated cave microbiome
    • Bhullar, K., et al. Antibiotic resistance is prevalent in an isolated cave microbiome. PLoS ONE 7, e34953 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e34953
    • Bhullar, K.1
  • 8
    • 84880714264 scopus 로고    scopus 로고
    • Intrinsic antibiotic resistance: Mechanisms, origins, challenges and solutions
    • Cox, G., & Wright, G. D. Intrinsic antibiotic resistance: mechanisms, origins, challenges and solutions. Int. J. Med. Microbiol. 303, 287-292 (2013).
    • (2013) Int. J. Med. Microbiol. , vol.303 , pp. 287-292
    • Cox, G.1    Wright, G.D.2
  • 9
    • 78149445856 scopus 로고    scopus 로고
    • The genomic enzymology of antibiotic resistance
    • Morar, M., & Wright, G. D. The genomic enzymology of antibiotic resistance. Annu. Rev. Genet. 44, 25-51 (2010).
    • (2010) Annu. Rev. Genet. , vol.44 , pp. 25-51
    • Morar, M.1    Wright, G.D.2
  • 10
    • 84924108668 scopus 로고    scopus 로고
    • Structural and molecular basis for resistance to aminoglycoside antibiotics by the adenylyltransferase ANT 2)-Ia
    • pii: e02180-14
    • Cox, G., Stogios, P. J., Savchenko, A., & Wright, G. D. Structural and molecular basis for resistance to aminoglycoside antibiotics by the adenylyltransferase ANT(2?)-Ia. MBio 6, pii: e02180-14 (2015).
    • (2015) MBio , vol.6
    • Cox, G.1    Stogios, P.J.2    Savchenko, A.3    Wright, G.D.4
  • 11
    • 71049134855 scopus 로고    scopus 로고
    • Structure and mechanism of the lincosamide antibiotic adenylyltransferase LinB
    • Morar, M., Bhullar, K., Hughes, D. W., Junop, M., & Wright, G. D. Structure and mechanism of the lincosamide antibiotic adenylyltransferase LinB. Structure 17, 1649-1659 (2009).
    • (2009) Structure , vol.17 , pp. 1649-1659
    • Morar, M.1    Bhullar, K.2    Hughes, D.W.3    Junop, M.4    Wright, G.D.5
  • 12
    • 84937763868 scopus 로고    scopus 로고
    • Structural and functional plasticity of antibiotic resistance nucleotidylyltransferases revealed by molecular characterization of lincosamide nucleotidylyltransferases lnu(A) and lnu D)
    • Stogios, P. J., et al. Structural and functional plasticity of antibiotic resistance nucleotidylyltransferases revealed by molecular characterization of lincosamide nucleotidylyltransferases lnu(A) and lnu(D). J. Mol. Biol. 427, 2229-2243 (2015).
    • (2015) J. Mol. Biol. , vol.427 , pp. 2229-2243
    • Stogios, P.J.1
  • 13
    • 0030846351 scopus 로고    scopus 로고
    • Characterization of gentamicin 2?-Nacetyltransferase from Providencia stuartii: Its use of peptidoglycan metabolites for acetylation of both aminoglycosides and peptidoglycan
    • Payie, K. G., & Clarke, A. J. Characterization of gentamicin 2?-Nacetyltransferase from Providencia stuartii: its use of peptidoglycan metabolites for acetylation of both aminoglycosides and peptidoglycan. J. Bacteriol. 179, 4106-4114 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 4106-4114
    • Payie, K.G.1    Clarke, A.J.2
  • 14
    • 0034213129 scopus 로고    scopus 로고
    • The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism
    • Izard, T., & Ellis, J. The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism. EMBO J. 19, 2690-2700 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2690-2700
    • Izard, T.1    Ellis, J.2
  • 15
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon, W. C., et al. Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89, 887-895 (1997).
    • (1997) Cell , vol.89 , pp. 887-895
    • Hon, W.C.1
  • 16
    • 0034872155 scopus 로고    scopus 로고
    • Active site labeling of the gentamicin resistance enzyme AAC 6?)-APH 2) by the lipid kinase inhibitor wortmannin
    • Boehr, D. D., Lane, W. S., & Wright, G. D. Active site labeling of the gentamicin resistance enzyme AAC(6?)-APH(2) by the lipid kinase inhibitor wortmannin. Chem. Biol. 8, 791-800 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 791-800
    • Boehr, D.D.1    Lane, W.S.2    Wright, G.D.3
  • 18
    • 0032466234 scopus 로고    scopus 로고
    • Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update
    • Ramaswamy, S., & Musser, J. M. Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update. Tuber. Lung Dis. 79, 3-29 (1998).
    • (1998) Tuber. Lung Dis. , vol.79 , pp. 3-29
    • Ramaswamy, S.1    Musser, J.M.2
  • 19
    • 84921730366 scopus 로고    scopus 로고
    • Resistance to rifampicin: A review
    • Goldstein, B. P. Resistance to rifampicin: a review. J. Antibiot. (Tokyo) 67, 625-630 (2014).
    • (2014) J. Antibiot. (Tokyo) , vol.67 , pp. 625-630
    • Goldstein, B.P.1
  • 20
    • 84866309704 scopus 로고    scopus 로고
    • Characterization of a rifampin-inactivating glycosyltransferase from a screen of environmental actinomycetes
    • Spanogiannopoulos, P., Thaker, M., Koteva, K., Waglechner, N., & Wright, G. D. Characterization of a rifampin-inactivating glycosyltransferase from a screen of environmental actinomycetes. Antimicrob. Agents Chemother. 56, 5061-5069 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5061-5069
    • Spanogiannopoulos, P.1    Thaker, M.2    Koteva, K.3    Waglechner, N.4    Wright, G.D.5
  • 21
    • 42449159361 scopus 로고    scopus 로고
    • Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr
    • Baysarowich, J., et al. Rifamycin antibiotic resistance by ADP-ribosylation: structure and diversity of Arr. Proc. Natl Acad. Sci. USA 105, 4886-4891 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 4886-4891
    • Baysarowich, J.1
  • 22
    • 77951768374 scopus 로고    scopus 로고
    • Resistance to rifampicin: At the crossroads between ecological, genomic and medical concerns
    • Tupin, A., et al. Resistance to rifampicin: at the crossroads between ecological, genomic and medical concerns. Int. J. Antimicrob. Agents 35, 519-523 (2010).
    • (2010) Int. J. Antimicrob. Agents , vol.35 , pp. 519-523
    • Tupin, A.1
  • 23
    • 84900493268 scopus 로고    scopus 로고
    • A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria
    • Spanogiannopoulos, P., Waglechner, N., Koteva, K., & Wright, G. D. A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria. Proc. Natl Acad. Sci. USA 111, 7102-7107
    • Proc. Natl Acad. Sci. USA , vol.111 , pp. 7102-7107
    • Spanogiannopoulos, P.1    Waglechner, N.2    Koteva, K.3    Wright, G.D.4
  • 24
    • 84868152309 scopus 로고    scopus 로고
    • Context matters-The complex interplay between resistome genotypes and resistance phenotypes
    • Dantas, G., & Sommer, M. O. Context matters-The complex interplay between resistome genotypes and resistance phenotypes. Curr. Opin. Microbiol. 15, 577-582 (2012).
    • (2012) Curr. Opin. Microbiol. , Issue.15 , pp. 577-582
    • Dantas, G.1    Sommer, M.O.2
  • 27
    • 0036259736 scopus 로고    scopus 로고
    • Detection of plasmid-mediated AmpC betalactamase genes in clinical isolates by using multiplex PCR
    • Perez-Perez, F. J., & Hanson, N. D. Detection of plasmid-mediated AmpC betalactamase genes in clinical isolates by using multiplex PCR. J. Clin. Microbiol. 40, 2153-2162 (2002).
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 2153-2162
    • Perez-Perez, F.J.1    Hanson, N.D.2
  • 28
    • 0014201723 scopus 로고
    • The mechanism of the phosphoenolpyruvate synthase reaction
    • Cooper, R. A., & Kornberg, H. L. The mechanism of the phosphoenolpyruvate synthase reaction. Biochim. Biophys. Acta 141, 211-213 (1967).
    • (1967) Biochim. Biophys. Acta , vol.141 , pp. 211-213
    • Cooper, R.A.1    Kornberg, H.L.2
  • 29
    • 0014369801 scopus 로고    scopus 로고
    • The mechanism of the pyruvate, phosphate dikinase reaction
    • Evans, H. J., & Wood, H. G. The mechanism of the pyruvate, phosphate dikinase reaction. Proc. Natl Acad. Sci. USA 61, 1448-1453
    • Proc. Natl Acad. Sci. USA , vol.61 , pp. 1448-1453
    • Evans, H.J.1    Wood, H.G.2
  • 30
    • 0037154102 scopus 로고    scopus 로고
    • Pyruvate site of pyruvate phosphate dikinase: Crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis
    • Herzberg, O., et al. Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis. Biochemistry 41, 780-787 (2002).
    • (2002) Biochemistry , vol.41 , pp. 780-787
    • Herzberg, O.1
  • 31
    • 37349033588 scopus 로고    scopus 로고
    • Swiveling domain mechanism in pyruvate phosphate dikinase
    • Lim, K., et al. Swiveling domain mechanism in pyruvate phosphate dikinase. Biochemistry 46, 14845-14853 (2007).
    • (2007) Biochemistry , vol.46 , pp. 14845-14853
    • Lim, K.1
  • 33
    • 0029911754 scopus 로고    scopus 로고
    • Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites
    • Herzberg, O., et al. Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites. Proc. Natl Acad. Sci. USA 93, 2652-2657 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2652-2657
    • Herzberg, O.1
  • 34
    • 0035813214 scopus 로고    scopus 로고
    • Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase
    • Ye, D., et al. Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase. J. Biol. Chem. 276, 37630-37639 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37630-37639
    • Ye, D.1
  • 35
    • 0029185933 scopus 로고
    • CRYSOL-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., & Koch, M. H. J. CRYSOL-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 36
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-Angle X-ray scattering
    • Bernado, P., Mylonas, E., Petoukhov, M. V., Blackledge, M., & Svergun, D. I. Structural characterization of flexible proteins using small-Angle X-ray scattering. J. Am. Chem. Soc. 129, 5656-5664 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 37
    • 84936847118 scopus 로고    scopus 로고
    • Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering
    • Tria, G., Mertens, H. D., Kachala, M., & Svergun, D. I. Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering. IUCr J. 26, 207-217 (2015).
    • (2015) IUCr J. , vol.26 , pp. 207-217
    • Tria, G.1    Mertens, H.D.2    Kachala, M.3    Svergun, D.I.4
  • 38
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase systemrelated protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., Francke, C., & Postma, P. W. How phosphotransferase systemrelated protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 70, 939-1031 (2006).
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 39
    • 0000186326 scopus 로고
    • Phosphate bound to histidine in a protein as an intermediate in a novel phospho-Transferase system
    • Kundig, W., Ghosh, S., & Roseman, S. Phosphate bound to histidine in a protein as an intermediate in a novel phospho-Transferase system. Proc. Natl Acad. Sci. USA 52, 1067-1074 (1964).
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 1067-1074
    • Kundig, W.1    Ghosh, S.2    Roseman, S.3
  • 40
    • 0035702148 scopus 로고    scopus 로고
    • Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism
    • Kotrba, P., Inui, M., & Yukawa, H. Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism. J. Biosci. Bioeng. 92, 502-517 (2001).
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 502-517
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 41
    • 13444291928 scopus 로고    scopus 로고
    • Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion
    • Nakanishi, T., Nakatsu, T., Matsuoka, M., Sakata, K., & Kato, H. Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion. Biochemistry 44, 1136-1144 (2005).
    • (2005) Biochemistry , vol.44 , pp. 1136-1144
    • Nakanishi, T.1    Nakatsu, T.2    Matsuoka, M.3    Sakata, K.4    Kato, H.5
  • 42
    • 33846059668 scopus 로고    scopus 로고
    • The generation of new protein functions by the combination of domains
    • Bashton, M., & Chothia, C. The generation of new protein functions by the combination of domains. Structure 15, 85-99 (2007).
    • (2007) Structure , vol.15 , pp. 85-99
    • Bashton, M.1    Chothia, C.2
  • 43
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J. A., & Babbitt, P. C. Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies. Annu. Rev. Biochem. 70, 209-246 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 44
    • 0034883978 scopus 로고    scopus 로고
    • Divergence of function in sequence-related groups of Escherichia coli proteins
    • Nahum, L. A., & Riley, M. Divergence of function in sequence-related groups of Escherichia coli proteins. Genome Res. 11, 1375-1381 (2001).
    • (2001) Genome Res. , vol.11 , pp. 1375-1381
    • Nahum, L.A.1    Riley, M.2
  • 45
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., & Chruszcz, M. HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62, 859-866 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 47
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D., et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 48
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D., et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 50
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenstrom, P.2
  • 51
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., & Henrick, K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 52
    • 78651338019 scopus 로고    scopus 로고
    • Extending CATH: Increasing coverage of the protein structure universe and linking structure with function
    • Cuff, A. L., et al. Extending CATH: increasing coverage of the protein structure universe and linking structure with function. Nucleic Acids Res. 39, D420-D426 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. D420-D426
    • Cuff, A.L.1
  • 53
    • 0030777303 scopus 로고    scopus 로고
    • CATH-A hierarchic classification of protein domain structures
    • Orengo, C. A., et al. CATH-A hierarchic classification of protein domain structures. Structure 5, 1093-1108 (1997).
    • (1997) Structure , vol.5 , pp. 1093-1108
    • Orengo, C.A.1
  • 56
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-Angle scattering
    • Rambo, R. P., & Tainer, J. A. Accurate assessment of mass, models and resolution by small-Angle scattering. Nature 496, 477-481
    • Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 57
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., & Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-2953 (2001).
    • (2001) Biophys. J. , Issue.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3


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