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Volumn 1, Issue 4, 2015, Pages

Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE;

EID: 85016596260     PISSN: None     EISSN: 23752548     Source Type: Journal    
DOI: 10.1126/sciadv.1500106     Document Type: Article
Times cited : (227)

References (53)
  • 1
    • 84871725540 scopus 로고    scopus 로고
    • Infectious disease: TB’s revenge
    • L. Phillips, Infectious disease: TB’s revenge. Nature 493, 14–16 (2013).
    • (2013) Nature , vol.493 , pp. 14-16
    • Phillips, L.1
  • 2
    • 84877100401 scopus 로고    scopus 로고
    • World Health Organisation, World Health Organisation, Geneva
    • World Health Organisation, WHO Global Tuberculosis Report 2013 (World Health Organisation, Geneva, 2013).
    • (2013) WHO Global Tuberculosis Report 2013
  • 3
    • 79251589638 scopus 로고    scopus 로고
    • The challenge of new drug discovery for tuberculosis
    • A. Koul, E. Arnoult, N. Lounis, J. Guillemont, K. Andries, The challenge of new drug discovery for tuberculosis. Nature 469, 483–490 (2011).
    • (2011) Nature , vol.469 , pp. 483-490
    • Koul, A.1    Arnoult, E.2    Lounis, N.3    Guillemont, J.4    Andries, K.5
  • 5
    • 84873120174 scopus 로고    scopus 로고
    • The ATP synthase: The understood, the uncertain and the unknown
    • J. E. Walker, The ATP synthase: The understood, the uncertain and the unknown. Biochem. Soc. Trans. 41, 1–16 (2013).
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1-16
    • Walker, J.E.1
  • 6
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase—A splendid molecular machine
    • P. D. Boyer, The ATP synthase—A splendid molecular machine. Annu. Rev. Biochem. 66, 717–749 (1997).
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 10
    • 21844435978 scopus 로고    scopus 로고
    • o-ATP synthase of Mycobacterium smegmatis is essential for growth
    • o-ATP synthase of Mycobacterium smegmatis is essential for growth. J. Bacteriol. 187, 5023–5028 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 5023-5028
    • Tran, S.L.1    Cook, G.M.2
  • 13
    • 34248545958 scopus 로고    scopus 로고
    • A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910
    • M. R. de Jonge, L. H. Koymans, J. E. Guillemont, A. Koul, K. Andries, A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 67, 971–980 (2007).
    • (2007) Proteins , vol.67 , pp. 971-980
    • De Jonge, M.R.1    Koymans, L.H.2    Guillemont, J.E.3    Koul, A.4    Andries, K.5
  • 14
    • 35848948213 scopus 로고    scopus 로고
    • In vitro antimycobacterial spectrum of a diarylquinoline ATP synthase inhibitor
    • E. Huitric, P. Verhasselt, K. Andries, S. E. Hoffner, In vitro antimycobacterial spectrum of a diarylquinoline ATP synthase inhibitor. Antimicrob. Agents Chemother. 51, 4202–4204 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 4202-4204
    • Huitric, E.1    Verhasselt, P.2    Andries, K.3    Hoffner, S.E.4
  • 17
    • 2742613426 scopus 로고
    • N,N′-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae
    • W. Sebald, W. Machleidt, E. Wachter, N,N′-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 77, 785–789 (1980).
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 785-789
    • Sebald, W.1    Machleidt, W.2    Wachter, E.3
  • 20
    • 78049239447 scopus 로고    scopus 로고
    • ATP synthase: From sequence to ring size to the P/O ratio
    • S. J. Ferguson, ATP synthase: From sequence to ring size to the P/O ratio. Proc. Natl. Acad. Sci. U.S.A. 107, 16755–16756 (2010).
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16755-16756
    • Ferguson, S.J.1
  • 22
    • 84865295687 scopus 로고    scopus 로고
    • A paradigmatic molecular machine
    • J. Frank, Ed. (Cambridge University Press, New York, )
    • T. Meier, J. D. Faraldo-Gómez, M. Börsch, A paradigmatic molecular machine, in Molecular Machines in Biology, J. Frank, Ed. (Cambridge University Press, New York, 2011), pp. 208–238.
    • (2011) Molecular Machines in Biology , pp. 208-238
    • Meier, T.1    Faraldo-Gómez, J.D.2    Börsch, M.3
  • 27
    • 84873572846 scopus 로고    scopus 로고
    • Techniques, tools and best practices for ligand electron-density analysis and results from their application to deposited crystal structures
    • E. Pozharski, C. X. Weichenberger, B. Rupp, Techniques, tools and best practices for ligand electron-density analysis and results from their application to deposited crystal structures. Acta Crystallogr. D Biol. Crystallogr. 69, 150–167 (2013).
    • (2013) Acta Crystallogr. D Biol. Crystallogr. , vol.69 , pp. 150-167
    • Pozharski, E.1    Weichenberger, C.X.2    Rupp, B.3
  • 28
    • 80051850771 scopus 로고    scopus 로고
    • Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase
    • A. C. Haagsma, I. Podasca, A. Koul, K. Andries, J. Guillemont, H. Lill, D. Bald, Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase. PLOS One 6, e23575 (2011).
    • (2011) PLOS One , vol.6 , pp. e23575
    • Haagsma, A.C.1    Podasca, I.2    Koul, A.3    Andries, K.4    Guillemont, J.5    Lill, H.6    Bald, D.7
  • 29
    • 84860157680 scopus 로고    scopus 로고
    • New mutations in the mycobacterial ATP synthase: New insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure
    • E. Segala, W. Sougakoff, A. Nevejans-Chauffour, V. Jarlier, S. Petrella, New mutations in the mycobacterial ATP synthase: New insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure. Antimicrob. Agents Chemother. 56, 2326–2334 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 2326-2334
    • Segala, E.1    Sougakoff, W.2    Nevejans-Chauffour, A.3    Jarlier, V.4    Petrella, S.5
  • 32
    • 84901589020 scopus 로고    scopus 로고
    • The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle
    • L. Preiss, J. D. Langer, D. B. Hicks, J. Liu, Ö. Yildiz, T. A. Krulwich, T. Meier, The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle. Mol. Microbiol. 92, 973–984 (2014).
    • (2014) Mol. Microbiol. , vol.92 , pp. 973-984
    • Preiss, L.1    Langer, J.D.2    Hicks, D.B.3    Liu, J.4    Yildiz, Ö.5    Krulwich, T.A.6    Meier, T.7
  • 33
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • P. Dauber-Osguthorpe, V. A. Roberts, D. J. Osguthorpe, J. Wolff, M. Genest, A. T. Hagler, Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins 4, 31–47 (1988).
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 34
    • 2942659093 scopus 로고    scopus 로고
    • Standard free energy of releasing a localized water molecule from the binding pockets of proteins: Double-decoupling method
    • D. Hamelberg, J. A. McCammon, Standard free energy of releasing a localized water molecule from the binding pockets of proteins: Double-decoupling method. J. Am. Chem. Soc. 126, 7683–7689 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7683-7689
    • Hamelberg, D.1    McCammon, J.A.2
  • 35
    • 70350315092 scopus 로고    scopus 로고
    • Energetics of displacing water molecules from protein binding sites: Consequences for ligand optimization
    • J. Michel, J. Tirado-Rives, W. L. Jorgensen, Energetics of displacing water molecules from protein binding sites: Consequences for ligand optimization. J. Am. Chem. Soc. 131, 15403–15411 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15403-15411
    • Michel, J.1    Tirado-Rives, J.2    Jorgensen, W.L.3
  • 36
    • 70349828967 scopus 로고    scopus 로고
    • High-resolution structure of the rotor ring of a proton-dependent ATP synthase
    • D. Pogoryelov, Ö. Yildiz, J. D. Faraldo-Gómez, T. Meier, High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat. Struct. Mol. Biol. 16, 1068–1073 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1068-1073
    • Pogoryelov, D.1    Yildiz, Ö.2    Faraldo-Gómez, J.D.3    Meier, T.4
  • 37
    • 0035043346 scopus 로고    scopus 로고
    • Intracellular pH regulation by Mycobacterium smegmatis and Mycobacterium bovis BCG
    • M. Rao, T. L. Streur, F. E. Aldwell, G. M. Cook, Intracellular pH regulation by Mycobacterium smegmatis and Mycobacterium bovis BCG. Microbiology 147, 1017–1024 (2001).
    • (2001) Microbiology , vol.147 , pp. 1017-1024
    • Rao, M.1    Streur, T.L.2    Aldwell, F.E.3    Cook, G.M.4
  • 38
    • 50149113470 scopus 로고    scopus 로고
    • The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis
    • S. P. Rao, S. Alonso, L. Rand, T. Dick, K. Pethe, The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 105, 11945–11950 (2008).
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11945-11950
    • Rao, S.P.1    Alonso, S.2    Rand, L.3    Dick, T.4    Pethe, K.5
  • 41
    • 0027340171 scopus 로고
    • + concentration: Probing the binding site for the coupling ions
    • + concentration: Probing the binding site for the coupling ions. Biochemistry 32, 10378–10386 (1993).
    • (1993) Biochemistry , vol.32 , pp. 10378-10386
    • Kluge, C.1    Dimroth, P.2
  • 43
    • 84927628815 scopus 로고    scopus 로고
    • Horizontal membrane-intrinsic a-helices in the stator a-subunit of an F-type ATP synthase
    • M. Allegretti, N. Klusch, D. J. Mills, J. Vonck, W. Kühlbrandt, K. M. Davies, Horizontal membrane-intrinsic a-helices in the stator a-subunit of an F-type ATP synthase. Nature 10.1038/nature14185 (2015).
    • (2015) Nature
    • Allegretti, M.1    Klusch, N.2    Mills, D.J.3    Vonck, J.4    Kühlbrandt, W.5    Davies, K.M.6
  • 46
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795–800 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 47
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • A. J. McCoy, Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32–41 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 51
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • 29
    • G. Vriend, WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8, 52–56, 29 (1990).
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 52
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • A. C. Wallace, R. A. Laskowski, J. M. Thornton, LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127–134 (1995).
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 53
    • 84961977344 scopus 로고    scopus 로고
    • On the interaction of aliphatic amines and ammonium ions with carboxylic acids in solution and in receptor pockets
    • P. I. Nagy, P. W. Erhardt, On the interaction of aliphatic amines and ammonium ions with carboxylic acids in solution and in receptor pockets. J. Phys. Chem. B 116, 5425–5436 (2012).
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5425-5436
    • Nagy, P.I.1    Erhardt, P.W.2


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