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Volumn 91, Issue 5, 2014, Pages 950-964

Structure of the bacterial type II NADH dehydrogenase: A monotopic membrane protein with an essential role in energy generation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FLAVINE ADENINE NUCLEOTIDE; FUNGAL ENZYME; HOMODIMER; MEMBRANE PROTEIN; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TYPE II NADH DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 84896733799     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12507     Document Type: Article
Times cited : (101)

References (45)
  • 2
    • 0030462751 scopus 로고    scopus 로고
    • Inhibition of the respiration of multi-drug resistant clinical isolates of Mycobacterium tuberculosis by thioridazine: potential use for initial therapy of freshly diagnosed tuberculosis
    • Amaral, L., Kristiansen, J.E., Abebe, L.S., and Millett, W. (1996) Inhibition of the respiration of multi-drug resistant clinical isolates of Mycobacterium tuberculosis by thioridazine: potential use for initial therapy of freshly diagnosed tuberculosis. J Antimicrob Chemother 38: 1049-1053.
    • (1996) J Antimicrob Chemother , vol.38 , pp. 1049-1053
    • Amaral, L.1    Kristiansen, J.E.2    Abebe, L.S.3    Millett, W.4
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Bailey, S. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
    • Bailey, S.1
  • 4
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., and McCammon, J.A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98: 10037-10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 5
    • 33646446147 scopus 로고    scopus 로고
    • Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria
    • Biagini, G.A., Viriyavejakul, P., O'Neill, P.M., Bray, P.G., and Ward, S.A. (2006) Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria. Antimicrob Agents Chemother 50: 1841-1851.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1841-1851
    • Biagini, G.A.1    Viriyavejakul, P.2    O'Neill, P.M.3    Bray, P.G.4    Ward, S.A.5
  • 6
    • 0018993676 scopus 로고
    • The kinetic mechanism of xanthine dehydrogenase and related enzymes
    • Coughlan, M.P., and Rajagopalan, K.V. (1980) The kinetic mechanism of xanthine dehydrogenase and related enzymes. Eur J Biochem 105: 81-84.
    • (1980) Eur J Biochem , vol.105 , pp. 81-84
    • Coughlan, M.P.1    Rajagopalan, K.V.2
  • 8
    • 79957592606 scopus 로고    scopus 로고
    • Improved molecular replacement by density- and energy-guided protein structure optimization
    • DiMaio, F., Terwilliger, T.C., Read, R.J., Wlodawer, A., Oberdorfer, G., Wagner, U., etal. (2011) Improved molecular replacement by density- and energy-guided protein structure optimization. Nature 473: 540-543.
    • (2011) Nature , vol.473 , pp. 540-543
    • DiMaio, F.1    Terwilliger, T.C.2    Read, R.J.3    Wlodawer, A.4    Oberdorfer, G.5    Wagner, U.6
  • 10
    • 13544275022 scopus 로고    scopus 로고
    • HDQ (1-hydroxy-2-dodecyl-4(1H)quinolone), a high affinity inhibitor for mitochondrial alternative NADH dehydrogenase
    • Eschemann, A., Galkin, A., Oettmeier, W., Brandt, U., and Kerscher, S. (2005) HDQ (1-hydroxy-2-dodecyl-4(1H)quinolone), a high affinity inhibitor for mitochondrial alternative NADH dehydrogenase. J Biol Chem 280: 3138-3142.
    • (2005) J Biol Chem , vol.280 , pp. 3138-3142
    • Eschemann, A.1    Galkin, A.2    Oettmeier, W.3    Brandt, U.4    Kerscher, S.5
  • 11
    • 84869083929 scopus 로고    scopus 로고
    • Structural insight into the type-II mitochondrial NADH dehydrogenases
    • Feng, Y., Li, W.F., Li, J., Wang, J.W., Ge, J.P., Xu, D., etal. (2012) Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature 491: 478-482.
    • (2012) Nature , vol.491 , pp. 478-482
    • Feng, Y.1    Li, W.F.2    Li, J.3    Wang, J.W.4    Ge, J.P.5    Xu, D.6
  • 12
    • 80053459692 scopus 로고    scopus 로고
    • High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism
    • Griffin, J.E., Gawronski, J.D., Dejesus, M.A., Ioerger, T.R., Akerley, B.J., and Sassetti, C.M. (2011) High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. PLoS Pathog 7: e1002251.
    • (2011) PLoS Pathog , vol.7
    • Griffin, J.E.1    Gawronski, J.D.2    Dejesus, M.A.3    Ioerger, T.R.4    Akerley, B.J.5    Sassetti, C.M.6
  • 13
    • 84866533591 scopus 로고    scopus 로고
    • The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates
    • Iwata, M., Lee, Y., Yamashita, T., Yagi, T., Iwata, S., Cameron, A.D., and Maher, M.J. (2012) The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates. Proc Natl Acad Sci USA 109: 15247-15252.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 15247-15252
    • Iwata, M.1    Lee, Y.2    Yamashita, T.3    Yagi, T.4    Iwata, S.5    Cameron, A.D.6    Maher, M.J.7
  • 14
    • 84874113282 scopus 로고    scopus 로고
    • Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3
    • Kabashima, Y., Sone, N., Kusumoto, T., and Sakamoto, J. (2013) Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3. J Bioenerg Biomembr 45: 131-136.
    • (2013) J Bioenerg Biomembr , vol.45 , pp. 131-136
    • Kabashima, Y.1    Sone, N.2    Kusumoto, T.3    Sakamoto, J.4
  • 16
    • 79961164756 scopus 로고    scopus 로고
    • Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus thermarum Strain TA2.A1
    • Kalamorz, F., Keis, S., McMillan, D.G.G., Olsson, K., Stanton, J.-A., Stockwell, P., etal. (2011) Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus thermarum Strain TA2.A1. J Bacteriol 193: 4290-4291.
    • (2011) J Bacteriol , vol.193 , pp. 4290-4291
    • Kalamorz, F.1    Keis, S.2    McMillan, D.G.G.3    Olsson, K.4    Stanton, J.-A.5    Stockwell, P.6
  • 17
    • 44449148400 scopus 로고    scopus 로고
    • The three families of respiratory NADH dehydrogenases
    • Schafer, G., and Penefsky, H.S. (eds). Berlin, Germany: Springer-Verlag Berlin
    • Kerscher, S., Drose, S., Zickermann, V., and Brandt, U. (2008) The three families of respiratory NADH dehydrogenases. In Results and Problems in Cell Differentiation. Schafer, G., and Penefsky, H.S. (eds). Berlin, Germany: Springer-Verlag Berlin, pp. 185-222.
    • (2008) Results and Problems in Cell Differentiation , pp. 185-222
    • Kerscher, S.1    Drose, S.2    Zickermann, V.3    Brandt, U.4
  • 18
    • 84890119929 scopus 로고    scopus 로고
    • A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli
    • Knuuti, J., Belevich, G., Sharma, V., Bloch, D.A., and Verkhovskaya, M. (2013) A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli. Mol Microbiol 90: 1190-1200.
    • (2013) Mol Microbiol , vol.90 , pp. 1190-1200
    • Knuuti, J.1    Belevich, G.2    Sharma, V.3    Bloch, D.A.4    Verkhovskaya, M.5
  • 19
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 20
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 58949085244 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • Liu, H., and Naismith, J.H. (2008) An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol 8: 91.
    • (2008) BMC Biotechnol , vol.8 , pp. 91
    • Liu, H.1    Naismith, J.H.2
  • 22
    • 43049110164 scopus 로고    scopus 로고
    • Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4
    • Liu, J., Krulwich, T.A., and Hicks, D.B. (2008) Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4. Biochim Biophys Acta 1777: 453-461.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 453-461
    • Liu, J.1    Krulwich, T.A.2    Hicks, D.B.3
  • 23
    • 0036775884 scopus 로고    scopus 로고
    • Characterization of a Mycobacterium tuberculosis H37Rv transposon library reveals insertions in 351 ORFs and mutants with altered virulence
    • McAdam, R.A., Quan, S., Smith, D.A., Bardarov, S., Betts, J.C., Cook, F.C., etal. (2002) Characterization of a Mycobacterium tuberculosis H37Rv transposon library reveals insertions in 351 ORFs and mutants with altered virulence. Microbiology 148: 2975-2986.
    • (2002) Microbiology , vol.148 , pp. 2975-2986
    • McAdam, R.A.1    Quan, S.2    Smith, D.A.3    Bardarov, S.4    Betts, J.C.5    Cook, F.C.6
  • 25
    • 67649872642 scopus 로고    scopus 로고
    • The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2009) The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106: 9625-9630.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 26
    • 77956504730 scopus 로고    scopus 로고
    • Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase
    • Marcia, M., Langer, J.D., Parcej, D., Vogel, V., Peng, G., and Michel, H. (2010) Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase. Biochim Biophys Acta 1798: 2114-2123.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2114-2123
    • Marcia, M.1    Langer, J.D.2    Parcej, D.3    Vogel, V.4    Peng, G.5    Michel, H.6
  • 27
    • 10344231976 scopus 로고    scopus 로고
    • New insights into Type II NAD(P)H: quinone oxidoreductases
    • Melo, A.M.P., Bandeiras, T.M., and Teixeira, M. (2004) New insights into Type II NAD(P)H: quinone oxidoreductases. Microbiol Mol Biol Rev 68: 603-616.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 603-616
    • Melo, A.M.P.1    Bandeiras, T.M.2    Teixeira, M.3
  • 28
    • 0031980127 scopus 로고    scopus 로고
    • NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis
    • Miesel, L., Weisbrod, T.R., Marcinkeviciene, J.A., Bittman, R., and Jacobs, W.R., Jr (1998) NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis. J Bacteriol 180: 2459-2467.
    • (1998) J Bacteriol , vol.180 , pp. 2459-2467
    • Miesel, L.1    Weisbrod, T.R.2    Marcinkeviciene, J.A.3    Bittman, R.4    Jacobs Jr., W.R.5
  • 29
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and Walker, J.E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J Mol Biol 260: 289-298.
    • (1996) J Mol Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 30
    • 81755173365 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli
    • Moxley, M.A., Tanner, J.J., and Becker, D.F. (2011) Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch Biochem Biophys 516: 113-120.
    • (2011) Arch Biochem Biophys , vol.516 , pp. 113-120
    • Moxley, M.A.1    Tanner, J.J.2    Becker, D.F.3
  • 32
    • 0037416986 scopus 로고    scopus 로고
    • Clinical concentrations of thioridazine kill intracellular multidrug-resistant Mycobacterium tuberculosis
    • Ordway, D., Viveiros, M., Leandro, C., Bettencourt, R., Almeida, J., Martins, M., etal. (2003) Clinical concentrations of thioridazine kill intracellular multidrug-resistant Mycobacterium tuberculosis. Antimicrob Agents Chemother 47: 917-922.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 917-922
    • Ordway, D.1    Viveiros, M.2    Leandro, C.3    Bettencourt, R.4    Almeida, J.5    Martins, M.6
  • 33
    • 50149113470 scopus 로고    scopus 로고
    • The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis
    • Rao, S.P., Alonso, S., Rand, L., Dick, T., and Pethe, K. (2008) The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis. Proc Natl Acad Sci USA 105: 11945-11950.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11945-11950
    • Rao, S.P.1    Alonso, S.2    Rand, L.3    Dick, T.4    Pethe, K.5
  • 34
    • 34247142732 scopus 로고    scopus 로고
    • Growth inhibition of Toxoplasma gondii and Plasmodium falciparum by nanomolar concentrations of 1-hydroxy-2-dodecyl-4(1H)quinolone, a high-affinity inhibitor of alternative (type II) NADH dehydrogenases
    • Saleh, A., Friesen, J., Baumeister, S., Gross, U., and Bohne, W. (2007) Growth inhibition of Toxoplasma gondii and Plasmodium falciparum by nanomolar concentrations of 1-hydroxy-2-dodecyl-4(1H)quinolone, a high-affinity inhibitor of alternative (type II) NADH dehydrogenases. Antimicrob Agents Chemother 51: 1217-1222.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1217-1222
    • Saleh, A.1    Friesen, J.2    Baumeister, S.3    Gross, U.4    Bohne, W.5
  • 35
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti, C.M., Boyd, D.H., and Rubin, E.J. (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48: 77-84.
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 37
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors
    • Unden, G., and Bongaerts, J. (1997) Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta 1320: 217-234.
    • (1997) Biochim Biophys Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 38
    • 12944255779 scopus 로고    scopus 로고
    • Altered NADH/NAD(+) ratio mediates coresistance to isoniazid and ethionamide in mycobacteria
    • Vilcheze, C., Weisbrod, T.R., Chen, B., Kremer, L., Hazbon, M.H., Wang, F., etal. (2005) Altered NADH/NAD(+) ratio mediates coresistance to isoniazid and ethionamide in mycobacteria. Antimicrob Agents Chemother 49: 708-720.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 708-720
    • Vilcheze, C.1    Weisbrod, T.R.2    Chen, B.3    Kremer, L.4    Hazbon, M.H.5    Wang, F.6
  • 40
    • 20144385739 scopus 로고    scopus 로고
    • Inhibitors of type II NADH:menaquinone oxidoreductase represent a class of antitubercular drugs
    • Weinstein, E.A., Yano, T., Li, L.S., Avarbock, D., Avarbock, A., Helm, D., etal. (2005) Inhibitors of type II NADH:menaquinone oxidoreductase represent a class of antitubercular drugs. Proc Natl Acad Sci USA 102: 4548-4553.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4548-4553
    • Weinstein, E.A.1    Yano, T.2    Li, L.S.3    Avarbock, D.4    Avarbock, A.5    Helm, D.6
  • 41
    • 34248163742 scopus 로고    scopus 로고
    • Roles of bound quinone in the single subunit NADH-quinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae
    • Yamashita, T., Nakamaru-Ogiso, E., Miyoshi, H., Matsuno-Yagi, A., and Yagi, T. (2007) Roles of bound quinone in the single subunit NADH-quinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae. J Biol Chem 282: 6012-6020.
    • (2007) J Biol Chem , vol.282 , pp. 6012-6020
    • Yamashita, T.1    Nakamaru-Ogiso, E.2    Miyoshi, H.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 42
    • 79953200453 scopus 로고    scopus 로고
    • Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae: evidence for a ternary complex mechanism
    • Yang, Y., Yamashita, T., Nakamaru-Ogiso, E., Hashimoto, T., Murai, M., Igarashi, J., etal. (2011) Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae: evidence for a ternary complex mechanism. J Biol Chem 286: 9287-9297.
    • (2011) J Biol Chem , vol.286 , pp. 9287-9297
    • Yang, Y.1    Yamashita, T.2    Nakamaru-Ogiso, E.3    Hashimoto, T.4    Murai, M.5    Igarashi, J.6
  • 43
    • 33744957049 scopus 로고    scopus 로고
    • Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2)
    • Yano, T., Li, L.S., Weinstein, E., Teh, J.S., and Rubin, H. (2006) Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2). J Biol Chem 281: 11456-11463.
    • (2006) J Biol Chem , vol.281 , pp. 11456-11463
    • Yano, T.1    Li, L.S.2    Weinstein, E.3    Teh, J.S.4    Rubin, H.5
  • 44
    • 42149117451 scopus 로고    scopus 로고
    • Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
    • Yeh, J.I., Chinte, U., and Du, S. (2008) Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc Natl Acad Sci USA 105: 3280-3285.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3280-3285
    • Yeh, J.I.1    Chinte, U.2    Du, S.3
  • 45
    • 33750814320 scopus 로고    scopus 로고
    • Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool
    • Zhang, J., Frerman, F.E., and Kim, J.-J.P. (2006) Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proc Natl Acad Sci USA 103: 16212-16217.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16212-16217
    • Zhang, J.1    Frerman, F.E.2    Kim, J.-J.3


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