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Volumn 1848, Issue 12, 2015, Pages 3158-3165

Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study

Author keywords

ABC transporter; LmrA; MAS NMR; Nucleotide binding; Protein dynamics; Solution NMR

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; LMRA PROTEIN; LYSINE; NUCLEOTIDE; UNCLASSIFIED DRUG; LMRA PROTEIN, LACTOCOCCUS LACTIS; MULTIDRUG RESISTANCE PROTEIN; PROTEIN BINDING;

EID: 84944263718     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2015.10.003     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 35648963623 scopus 로고    scopus 로고
    • ABC transporters: How small machines do a big job
    • A.L. Davidson, and P.C. Maloney ABC transporters: how small machines do a big job Trends Microbiol. 15 2007 448 455
    • (2007) Trends Microbiol. , vol.15 , pp. 448-455
    • Davidson, A.L.1    Maloney, P.C.2
  • 7
    • 36849090063 scopus 로고    scopus 로고
    • MAS solid-state NMR studies on the multidrug transporter EmrE
    • V. Agarwal, U. Fink, S. Schuldiner, and B. Reif MAS solid-state NMR studies on the multidrug transporter EmrE Biochim. Biophys. Acta 1768 2007 3036 3043
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3036-3043
    • Agarwal, V.1    Fink, U.2    Schuldiner, S.3    Reif, B.4
  • 8
    • 77956218757 scopus 로고    scopus 로고
    • Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes
    • S.T. Amadi, H.A. Koteiche, S. Mishra, and H.S. Mchaourab Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes J. Biolumin. Chemilumin. 285 2010 26710 26718
    • (2010) J. Biolumin. Chemilumin. , vol.285 , pp. 26710-26718
    • Amadi, S.T.1    Koteiche, H.A.2    Mishra, S.3    Mchaourab, H.S.4
  • 9
    • 36749045119 scopus 로고    scopus 로고
    • Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli
    • Y. Takatsuka, and H. Nikaido Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli J. Bacteriol. 189 2007 8677 8684
    • (2007) J. Bacteriol. , vol.189 , pp. 8677-8684
    • Takatsuka, Y.1    Nikaido, H.2
  • 11
    • 84863586032 scopus 로고    scopus 로고
    • Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations
    • S. Mehmood, C. Domene, E. Forest, and J.M. Jault Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations Proc. Natl. Acad. Sci. U. S. A. 109 2012 10832 10836
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 10832-10836
    • Mehmood, S.1    Domene, C.2    Forest, E.3    Jault, J.M.4
  • 13
    • 84922342044 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • (eCollection 2015)
    • S. Wilkens Structure and mechanism of ABC transporters F1000Prime Rep. 7 2015 10.12703/P7-14 (eCollection 2015)
    • (2015) F1000Prime Rep. , vol.7
    • Wilkens, S.1
  • 14
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, and N.J. Gay Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold EMBO J. 1 8 1982 945 951
    • (1982) EMBO J. , vol.1 , Issue.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 15
    • 77953229777 scopus 로고    scopus 로고
    • Substitution of the Walker A lysine by arginine in the nucleotide-binding domains of sulphonylurea receptor SUR2B: Effects on ligand binding and channel activity
    • T. Amann, S. Schell, P. Kühner, M. Winkler, M. Schwanstecher, U. Russ, and U. Quast Substitution of the Walker A lysine by arginine in the nucleotide-binding domains of sulphonylurea receptor SUR2B: effects on ligand binding and channel activity Naunyn Schmiedeberg's Arch. Pharmacol. 381 2010 507 516
    • (2010) Naunyn Schmiedeberg's Arch. Pharmacol. , vol.381 , pp. 507-516
    • Amann, T.1    Schell, S.2    Kühner, P.3    Winkler, M.4    Schwanstecher, M.5    Russ, U.6    Quast, U.7
  • 16
  • 17
    • 53049103551 scopus 로고    scopus 로고
    • Caught in the act: ATP hydrolysis of an ABC-multidrug transporter followed by real-time magic angle spinning NMR
    • U.A. Hellmich, W. Haase, S. Velamakanni, H.W. van Veen, and C. Glaubitz Caught in the act: ATP hydrolysis of an ABC-multidrug transporter followed by real-time magic angle spinning NMR FEBS Lett. 582 2008 3557 3562
    • (2008) FEBS Lett. , vol.582 , pp. 3557-3562
    • Hellmich, U.A.1    Haase, W.2    Velamakanni, S.3    Van Veen, H.W.4    Glaubitz, C.5
  • 18
    • 84929590364 scopus 로고    scopus 로고
    • A transporter motor taken apart: Flexibility in the nucleotide binding domains of a heterodimeric ABC exporter
    • M.A. Bukowska, M. Hohl, E.R. Geertsma, L.M. Hürlimann, M.G. Grütter, and M.A. Seeger A transporter motor taken apart: flexibility in the nucleotide binding domains of a heterodimeric ABC exporter Biochemistry 54 2015 3086 3099
    • (2015) Biochemistry , vol.54 , pp. 3086-3099
    • Bukowska, M.A.1    Hohl, M.2    Geertsma, E.R.3    Hürlimann, L.M.4    Grütter, M.G.5    Seeger, M.A.6
  • 19
    • 79953183043 scopus 로고    scopus 로고
    • Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from thermus thermophiles
    • A. Zutz, J. Hoffmann, U.A. Hellmich, C. Glaubitz, B. Ludwig, B. Brutschy, and R. Tampé Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from thermus thermophiles J. Biol. Chem. 286 2011 7104 7115
    • (2011) J. Biol. Chem. , vol.286 , pp. 7104-7115
    • Zutz, A.1    Hoffmann, J.2    Hellmich, U.A.3    Glaubitz, C.4    Ludwig, B.5    Brutschy, B.6    Tampé, R.7
  • 20
    • 0034460877 scopus 로고    scopus 로고
    • Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis
    • S. Sharma, and A.L. Davidson Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis J. Bacteriol. 182 2000 6570 6576
    • (2000) J. Bacteriol. , vol.182 , pp. 6570-6576
    • Sharma, S.1    Davidson, A.L.2
  • 21
    • 33749994338 scopus 로고    scopus 로고
    • Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter
    • P.L. Russell, and F.J. Sharom Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter Biochem. J. 99 2006 315 323
    • (2006) Biochem. J. , vol.99 , pp. 315-323
    • Russell, P.L.1    Sharom, F.J.2
  • 22
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • M. Hong, Y. Zhang, and F. Hu Membrane protein structure and dynamics from NMR spectroscopy Annu. Rev. Phys. Chem. 63 2012 1 24
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 23
    • 70349462902 scopus 로고    scopus 로고
    • NMR and EPR studies of membrane transporters
    • U.A. Hellmich, and C. Glaubitz NMR and EPR studies of membrane transporters Biol. Chem. 390 2009 815 834
    • (2009) Biol. Chem. , vol.390 , pp. 815-834
    • Hellmich, U.A.1    Glaubitz, C.2
  • 24
    • 84901368299 scopus 로고    scopus 로고
    • Characterization of membrane protein function by solid-state NMR spectroscopy
    • L.A. Baker, and M. Baldus Characterization of membrane protein function by solid-state NMR spectroscopy Curr. Opin. Struct. Biol. 27 2014 48 55
    • (2014) Curr. Opin. Struct. Biol. , vol.27 , pp. 48-55
    • Baker, L.A.1    Baldus, M.2
  • 25
    • 2942594347 scopus 로고    scopus 로고
    • Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies
    • A.J. Mason, A. Siarheyeva, W. Haase, M. Lorch, H.W. van Veen, and C. Glaubitz Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies FEBS Lett. 568 2004 117 121
    • (2004) FEBS Lett. , vol.568 , pp. 117-121
    • Mason, A.J.1    Siarheyeva, A.2    Haase, W.3    Lorch, M.4    Van Veen, H.W.5    Glaubitz, C.6
  • 26
    • 33947388784 scopus 로고    scopus 로고
    • Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance
    • A. Siarheyeva, J.J. Lopez, I. Lehner, U.A. Hellmich, H.W. van Veen, and C. Glaubitz Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance Biochemistry 46 2007 3075 3083
    • (2007) Biochemistry , vol.46 , pp. 3075-3083
    • Siarheyeva, A.1    Lopez, J.J.2    Lehner, I.3    Hellmich, U.A.4    Van Veen, H.W.5    Glaubitz, C.6
  • 31
    • 84858297845 scopus 로고    scopus 로고
    • Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state
    • U.A. Hellmich, E. Duchardt-Ferner, C. Glaubitz, and J. Wöhnert Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state Biomol. NMR Assign. 6 2012 69 73
    • (2012) Biomol. NMR Assign. , vol.6 , pp. 69-73
    • Hellmich, U.A.1    Duchardt-Ferner, E.2    Glaubitz, C.3    Wöhnert, J.4
  • 32
    • 77957010716 scopus 로고
    • Bacterial membranes
    • H.R. Kaback Bacterial membranes Methods Enzymol. 22 1971 99 120
    • (1971) Methods Enzymol. , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 33
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • A. Margolles, M. Putman, H.W. van Veen, and W.N. Konings The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids Biochemistry 38 1999 16298 16306
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 34
    • 53749101652 scopus 로고    scopus 로고
    • Functional role of transmembrane helix 6 in drug binding and transport by the ABC transporter MsbA
    • B. Woebking, S. Velamakanni, L. Federici, M.A. Seeger, S. Murakami, and H.W. van Veen Functional role of transmembrane helix 6 in drug binding and transport by the ABC transporter MsbA Biochemistry 47 2008 10904 10914
    • (2008) Biochemistry , vol.47 , pp. 10904-10914
    • Woebking, B.1    Velamakanni, S.2    Federici, L.3    Seeger, M.A.4    Murakami, S.5    Van Veen, H.W.6
  • 35
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • R.J. Dawson, and K.P. Locher Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP FEBS Lett. 581 2007 935 938
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 37
    • 64649100965 scopus 로고    scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • K.M. Pos Drug transport mechanism of the AcrB efflux pump Biochim. Biophys. Acta 1794 2009 782 793
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 782-793
    • Pos, K.M.1
  • 38
    • 37349115703 scopus 로고    scopus 로고
    • On the energy-dependence of Hoechst 33342 transport by the ABC transporter LmrA
    • H. Venter, S. Velamakanni, L. Balakrishnan, and H.W. Van Veen On the energy-dependence of Hoechst 33342 transport by the ABC transporter LmrA Biochem. Pharmacol. 75 2008 866 874
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 866-874
    • Venter, H.1    Velamakanni, S.2    Balakrishnan, L.3    Van Veen, H.W.4
  • 39
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Y. Wang, and O. Jardetzky Probability-based protein secondary structure identification using combined NMR chemical-shift data Protein Sci. 11 2002 852 861
    • (2002) Protein Sci. , vol.11 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 41
    • 0034818922 scopus 로고    scopus 로고
    • Drug transport by reconstituted P-glycoprotein in proteoliposomes. Effect of substrates and modulators, and dependence on bilayer phase state
    • P. Lu, R. Liu, and F.J. Sharom Drug transport by reconstituted P-glycoprotein in proteoliposomes. Effect of substrates and modulators, and dependence on bilayer phase state Eur. J. Biochem. 268 2001 1687 1697
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1687-1697
    • Lu, P.1    Liu, R.2    Sharom, F.J.3
  • 42
    • 52249103044 scopus 로고    scopus 로고
    • P-glycoprotein senses its substrates and the lateral membrane packing density: Consequences for the catalytic cycle
    • P. Aanismaa, E. Gatlik-Landwojtowicz, and A. Seelig P-glycoprotein senses its substrates and the lateral membrane packing density: consequences for the catalytic cycle Biochemistry 47 2008 10197 10207
    • (2008) Biochemistry , vol.47 , pp. 10197-10207
    • Aanismaa, P.1    Gatlik-Landwojtowicz, E.2    Seelig, A.3
  • 43
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • C.F. Higgins Multiple molecular mechanisms for multidrug resistance transporters Nature 446 2007 749 757
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 45
    • 70349785109 scopus 로고    scopus 로고
    • Conformational cycle of the ABC transporter MsbA in liposomes: Detailed analysis using double electron-electron resonance spectroscopy
    • P. Zou, M. Bortolus, and H.S. McHaourab Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy J. Mol. Biol. 393 2009 586 597
    • (2009) J. Mol. Biol. , vol.393 , pp. 586-597
    • Zou, P.1    Bortolus, M.2    McHaourab, H.S.3
  • 46
    • 84899646384 scopus 로고    scopus 로고
    • 3D cryo-electron reconstruction of BmrA, a bacterial multidrug ABC transporter in an inward-facing conformation and in a lipidic environment
    • P.F. Fribourg, M. Chami, C.O. Sorzano, F. Gubellini, R. Marabini, S. Marco, J.M. Jault, and D. Lévy 3D cryo-electron reconstruction of BmrA, a bacterial multidrug ABC transporter in an inward-facing conformation and in a lipidic environment J. Mol. Biol. 426 2014 2059 2069
    • (2014) J. Mol. Biol. , vol.426 , pp. 2059-2069
    • Fribourg, P.F.1    Chami, M.2    Sorzano, C.O.3    Gubellini, F.4    Marabini, R.5    Marco, S.6    Jault, J.M.7    Lévy, D.8
  • 47
    • 70349785154 scopus 로고    scopus 로고
    • Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA
    • P. Zou, and H.S. McHaourab Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA J. Mol. Biol. 393 2009 574 585
    • (2009) J. Mol. Biol. , vol.393 , pp. 574-585
    • Zou, P.1    McHaourab, H.S.2
  • 48
    • 0037162511 scopus 로고    scopus 로고
    • How are the ABC transporters energized?
    • H. Nikaido How are the ABC transporters energized? Proc. Natl. Acad. Sci. U. S. A. 99 2002 9609 9610
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9609-9610
    • Nikaido, H.1
  • 49
    • 84875833653 scopus 로고    scopus 로고
    • A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization
    • N. Tal, E. Ovcharenko, and O. Lewinson A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization Proc. Natl. Acad. Sci. U. S. A. 110 2013 5434 5439
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 5434-5439
    • Tal, N.1    Ovcharenko, E.2    Lewinson, O.3
  • 50
    • 84907683485 scopus 로고    scopus 로고
    • The Q loops of the human multidrug resistance transporter ABCB1 are necessary to couple drug binding to the ATP catalytic cycle
    • J.K. Zolnerciks, B.G. Akkaya, M. Snippe, P. Chiba, A. Seelig, and K.J. Linton The Q loops of the human multidrug resistance transporter ABCB1 are necessary to couple drug binding to the ATP catalytic cycle FASEB J. 28 2014 4335 4346
    • (2014) FASEB J. , vol.28 , pp. 4335-4346
    • Zolnerciks, J.K.1    Akkaya, B.G.2    Snippe, M.3    Chiba, P.4    Seelig, A.5    Linton, K.J.6


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