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Volumn 1666, Issue 1-2, 2004, Pages 2-18

Lipids in membrane protein structures

Author keywords

Cardiolipin; Lipid; Lipid protein interaction; Membrane protein; Phospholipid; X ray structure

Indexed keywords

CARDIOLIPIN; LIPID; LIPID BINDING PROTEIN; PORIN; PROTEIN;

EID: 7044274626     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.06.012     Document Type: Review
Times cited : (349)

References (104)
  • 1
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • T.J. Stevens, and IT. Arkin Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39 4 2000 417 420
    • (2000) Proteins , vol.39 , Issue.4 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 2
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • E. Perozo, D.M. Cortes, P. Sompornpisut, A. Kloda, and B. Martinac Open channel structure of MscL and the gating mechanism of mechanosensitive channels Nature 418 6901 2002 942 948
    • (2002) Nature , vol.418 , Issue.6901 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 3
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • I. Ubarretxena-Belandia, J.M. Baldwin, S. Schuldiner, and C.G. Tate Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer EMBO J. 22 23 2003 6175 6181
    • (2003) EMBO J. , vol.22 , Issue.23 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 4
    • 0024744871 scopus 로고
    • Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
    • N.A. Dencher, D. Dresselhaus, G. Zaccai, and G. Buldt Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction Proc Natl Acad Sci U. S. A. 86 20 1989 7876 7879
    • (1989) Proc Natl Acad Sci U. S. A. , vol.86 , Issue.20 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Buldt, G.4
  • 5
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • D. Stock, A.G. Leslie, and J.E. Walker Molecular architecture of the rotary motor in ATP synthase Science 286 5445 1999 1700 1705
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 8
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 6633 1997 569 572
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 9
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes?
    • D.A. Brown, and E. London Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? Biochem Biophys. Res. Commun. 240 1 1997 1 7
    • (1997) Biochem Biophys. Res. Commun. , vol.240 , Issue.1 , pp. 1-7
    • Brown, D.A.1    London, E.2
  • 10
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • D.A. Brown, and E. London Functions of lipid rafts in biological membranes Annu. Rev. Cell Dev. Biol. 14 1998 111 136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 11
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • K. Simons, and D. Toomre Lipid rafts and signal transduction Nat. Rev. Mol. Cell Biol. 1 1 2000 31 39
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , Issue.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 12
    • 0141828502 scopus 로고    scopus 로고
    • Use of detergents to study membrane rafts: The good, the bad, and the ugly
    • H. Shogomori, and D.A. Brown Use of detergents to study membrane rafts: the good, the bad, and the ugly Biol. Chem. 384 9 2003 1259 1263
    • (2003) Biol. Chem. , vol.384 , Issue.9 , pp. 1259-1263
    • Shogomori, H.1    Brown, D.A.2
  • 13
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • D. Marsh, and L.I. Horvath Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling Biochim. Biophys. Acta 1376 3 1998 267 296
    • (1998) Biochim. Biophys. Acta , vol.1376 , Issue.3 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 14
    • 0026758940 scopus 로고
    • Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy
    • M. Hayer-Hartl, H. Schagger, G. von Jagow, and K. Beyer Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy Eur. J. Biochem. 209 1 1992 423 430
    • (1992) Eur. J. Biochem. , vol.209 , Issue.1 , pp. 423-430
    • Hayer-Hartl, M.1    Schagger, H.2    Von Jagow, G.3    Beyer, K.4
  • 15
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • W. Dowhan Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66 1997 199 232
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 16
  • 17
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • C. Hunte, and H. Michel Crystallisation of membrane proteins mediated by antibody fragments Curr. Opin. Struct. Biol. 12 4 2002 503 508
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , Issue.4 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 19
  • 20
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • A.G. Lee Lipid-protein interactions in biological membranes: a structural perspective Biochim. Biophys. Acta 1612 1 2003 1 40
    • (2003) Biochim. Biophys. Acta , vol.1612 , Issue.1 , pp. 1-40
    • Lee, A.G.1
  • 21
    • 0035424669 scopus 로고    scopus 로고
    • High-resolution structures and dynamics of membrane protein-lipid complexes: A critique
    • E. Pebay-Peyroula, and J.P. Rosenbusch High-resolution structures and dynamics of membrane protein-lipid complexes: a critique Curr. Opin. Struct. Biol. 11 4 2001 427 432
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , Issue.4 , pp. 427-432
    • Pebay-Peyroula, E.1    Rosenbusch, J.P.2
  • 23
    • 0019320448 scopus 로고
    • Structural role of phospholipids in ubiquinol-cytochrome c reductase
    • C.A. Yu, and L. Yu Structural role of phospholipids in ubiquinol-cytochrome c reductase Biochemistry 19 25 1980 5715 5720
    • (1980) Biochemistry , vol.19 , Issue.25 , pp. 5715-5720
    • Yu, C.A.1    Yu, L.2
  • 25
    • 0028917485 scopus 로고
    • Lipid-protein interactions in the purple membrane: Structural specificity within the hydrophobic domain
    • V. Pomerleau, G. Harvey, and F. Boucher Lipid-protein interactions in the purple membrane: structural specificity within the hydrophobic domain Biochim. Biophys. Acta 1234 2 1995 221 224
    • (1995) Biochim. Biophys. Acta , vol.1234 , Issue.2 , pp. 221-224
    • Pomerleau, V.1    Harvey, G.2    Boucher, F.3
  • 27
    • 0023878031 scopus 로고
    • Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
    • T. de Vrije, R.L. de Swart, W. Dowhan, J. Tommassen, and B. de Kruijff Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes Nature 334 6178 1988 173 175
    • (1988) Nature , vol.334 , Issue.6178 , pp. 173-175
    • De Vrije, T.1    De Swart, R.L.2    Dowhan, W.3    Tommassen, J.4    De Kruijff, B.5
  • 28
    • 0034723287 scopus 로고    scopus 로고
    • Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase
    • C. van Does, J. Swaving, W. van Klompenburg, and A.J. Driessen Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase J. Biol. Chem. 275 4 2000 2472 2478
    • (2000) J. Biol. Chem. , vol.275 , Issue.4 , pp. 2472-2478
    • Van Does, C.1    Swaving, J.2    Van Klompenburg, W.3    Driessen, A.J.4
  • 29
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • G. von Heijne, and Y. Gavel Topogenic signals in integral membrane proteins Eur. J. Biochem. 174 4 1988 671 678
    • (1988) Eur. J. Biochem. , vol.174 , Issue.4 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 30
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • W. van Klompenburg, I. Nilsson, G. von Heijne, and B. de Kruijff Anionic phospholipids are determinants of membrane protein topology EMBO J. 16 14 1997 4261 4266
    • (1997) EMBO J. , vol.16 , Issue.14 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 31
    • 0028938736 scopus 로고
    • Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli
    • M. Bogdanov, and W. Dowhan Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli J. Biol. Chem. 270 2 1995 732 739
    • (1995) J. Biol. Chem. , vol.270 , Issue.2 , pp. 732-739
    • Bogdanov, M.1    Dowhan, W.2
  • 32
    • 0032530656 scopus 로고    scopus 로고
    • Phospholipid-assisted protein folding: Phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease
    • M. Bogdanov, and W. Dowhan Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease EMBO J. 17 18 1998 5255 5264
    • (1998) EMBO J. , vol.17 , Issue.18 , pp. 5255-5264
    • Bogdanov, M.1    Dowhan, W.2
  • 33
    • 0033617356 scopus 로고    scopus 로고
    • Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone
    • M. Bogdanov, M. Umeda, and W. Dowhan Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone J. Biol. Chem. 274 18 1999 12339 12345
    • (1999) J. Biol. Chem. , vol.274 , Issue.18 , pp. 12339-12345
    • Bogdanov, M.1    Umeda, M.2    Dowhan, W.3
  • 34
    • 0033601291 scopus 로고    scopus 로고
    • Lipid-assisted protein folding
    • M. Bogdanov, and W. Dowhan Lipid-assisted protein folding J. Biol. Chem. 274 52 1999 36827 36830
    • (1999) J. Biol. Chem. , vol.274 , Issue.52 , pp. 36827-36830
    • Bogdanov, M.1    Dowhan, W.2
  • 35
    • 0036566310 scopus 로고    scopus 로고
    • A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
    • M. Bogdanov, P.N. Heacock, and W. Dowhan A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition EMBO J. 21 9 2002 2107 2116
    • (2002) EMBO J. , vol.21 , Issue.9 , pp. 2107-2116
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 36
    • 0041352147 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane
    • J.P. Cartailler, and H. Luecke X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane Annu. Rev. Biophys. Biomol. Struct. 32 2003 285 310
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 285-310
    • Cartailler, J.P.1    Luecke, H.2
  • 37
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • R. Henderson, and P.N. Unwin Three-dimensional model of purple membrane obtained by electron microscopy Nature 257 5521 1975 28 32
    • (1975) Nature , vol.257 , Issue.5521 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 38
    • 0029620939 scopus 로고
    • Lipid location in deoxycholate-treated purple membrane at 2.6 Å
    • N. Grigorieff, E. Beckmann, and F. Zemlin Lipid location in deoxycholate-treated purple membrane at 2.6 Å J. Mol. Biol. 254 3 1995 404 415
    • (1995) J. Mol. Biol. , vol.254 , Issue.3 , pp. 404-415
    • Grigorieff, N.1    Beckmann, E.2    Zemlin, F.3
  • 39
    • 85047693143 scopus 로고
    • The ability of actinic light to modify the bacteriorhodopsin photocycle. Heterogeneity and/or photocooperativity?
    • R.I. Shrager, R.W. Hendler, and S. Bose The ability of actinic light to modify the bacteriorhodopsin photocycle. Heterogeneity and/or photocooperativity? Eur. J. Biochem. 229 3 1995 589 595
    • (1995) Eur. J. Biochem. , vol.229 , Issue.3 , pp. 589-595
    • Shrager, R.I.1    Hendler, R.W.2    Bose, S.3
  • 40
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • N. Grigorieff, T.A. Ceska, K.H. Downing, J.M. Baldwin, and R. Henderson Electron-crystallographic refinement of the structure of bacteriorhodopsin J. Mol. Biol. 259 3 1996 393 421
    • (1996) J. Mol. Biol. , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 41
    • 0002659282 scopus 로고    scopus 로고
    • Towards structural investigation on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR
    • H. Patzelt, A.S. Ulrich, H. Egbringhoff, P. Dux, and R. Ashurst Towards structural investigation on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR J. Biomol. NMR 10 1997 95 106
    • (1997) J. Biomol. NMR , vol.10 , pp. 95-106
    • Patzelt, H.1    Ulrich, A.S.2    Egbringhoff, H.3    Dux, P.4    Ashurst, R.5
  • 42
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • H. Belrhali, P. Nollert, A. Royant, C. Menzel, J.P. Rosenbusch, E.M. Landau, and E. Pebay-Peyroula Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution Structure Fold Des. 7 8 1999 909 917
    • (1999) Structure Fold Des. , vol.7 , Issue.8 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 45
    • 0018793910 scopus 로고
    • Spin-label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase
    • P.F. Knowles, A. Watts, and D. Marsh Spin-label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase Biochemistry 18 21 1979 4480 4487
    • (1979) Biochemistry , vol.18 , Issue.21 , pp. 4480-4487
    • Knowles, P.F.1    Watts, A.2    Marsh, D.3
  • 46
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • B.A. Lewis, and D.M. Engelman Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles J. Mol. Biol. 166 2 1983 211 217
    • (1983) J. Mol. Biol. , vol.166 , Issue.2 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 47
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • L.O. Essen, R. Siegert, W.D. Lehmann, and D. Oesterhelt Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. U. S. A. 1998 95
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , pp. 95
    • Essen, L.O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 48
    • 0032514725 scopus 로고    scopus 로고
    • Importance of specific native lipids in controlling the photocycle of bacteriorhodopsin
    • M.K. Joshi, S. Dracheva, A.K. Mukhopadhyay, S. Bose, and R.W. Hendler Importance of specific native lipids in controlling the photocycle of bacteriorhodopsin Biochemistry 37 41 1998 14463 14470
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14463-14470
    • Joshi, M.K.1    Dracheva, S.2    Mukhopadhyay, A.K.3    Bose, S.4    Hendler, R.W.5
  • 49
    • 0019888306 scopus 로고
    • Reconstitution of delipidated bacteriorhodopsin with endogenous polar lipids
    • C. Lind, B. Hojeberg, and H.G. Khorana Reconstitution of delipidated bacteriorhodopsin with endogenous polar lipids J. Biol. Chem. 256 16 1981 8298 8305
    • (1981) J. Biol. Chem. , vol.256 , Issue.16 , pp. 8298-8305
    • Lind, C.1    Hojeberg, B.2    Khorana, H.G.3
  • 50
    • 0027452052 scopus 로고
    • Lipid-protein interactions in crystals of plant light-harvesting complex
    • S. Nussberger, K. Dorr, D.N. Wang, and W. Kuhlbrandt Lipid-protein interactions in crystals of plant light-harvesting complex J. Mol. Biol. 234 2 1993 347 356
    • (1993) J. Mol. Biol. , vol.234 , Issue.2 , pp. 347-356
    • Nussberger, S.1    Dorr, K.2    Wang, D.N.3    Kuhlbrandt, W.4
  • 51
    • 0028049588 scopus 로고
    • Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex
    • S. Hobe, S. Prytulla, W. Kuhlbrandt, and H. Paulsen Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex EMBO J. 13 15 1994 3423 3429
    • (1994) EMBO J. , vol.13 , Issue.15 , pp. 3423-3429
    • Hobe, S.1    Prytulla, S.2    Kuhlbrandt, W.3    Paulsen, H.4
  • 52
    • 0026496915 scopus 로고
    • The primary structures of helices a to G of three new bacteriorhodopsin-like retinal proteins
    • J. Otomo, Y. Urabe, H. Tomioka, and H. Sasabe The primary structures of helices A to G of three new bacteriorhodopsin-like retinal proteins J. Gen. Microbiol. 138 Pt 11 1992 2389 2396
    • (1992) J. Gen. Microbiol. , vol.138 , Issue.11 , pp. 2389-2396
    • Otomo, J.1    Urabe, Y.2    Tomioka, H.3    Sasabe, H.4
  • 54
    • 0037077723 scopus 로고    scopus 로고
    • Influence of lipids on membrane assembly and stability of the potassium channel KcsA
    • A. van Dalen, S. Hegger, J.A. Killian, and B. de Kruijff Influence of lipids on membrane assembly and stability of the potassium channel KcsA FEBS Lett. 525 1-3 2002 33 38
    • (2002) FEBS Lett. , vol.525 , Issue.13 , pp. 33-38
    • Van Dalen, A.1    Hegger, S.2    Killian, J.A.3    De Kruijff, B.4
  • 56
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • P. Jordan, P. Fromme, H.T. Witt, O. Klukas, W. Saenger, and N. Krauss Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution Nature 411 6840 2001 909 917
    • (2001) Nature , vol.411 , Issue.6840 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 57
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , Issue.2 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 59
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • G. von Heijne Mitochondrial targeting sequences may form amphiphilic helices EMBO J. 5 6 1986 1335 1342
    • (1986) EMBO J. , vol.5 , Issue.6 , pp. 1335-1342
    • Von Heijne, G.1
  • 60
    • 0005384356 scopus 로고
    • Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
    • J. Deisenhofer, and H. Michel Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis EMBO J. 8 8 1989 2149 2170
    • (1989) EMBO J. , vol.8 , Issue.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 61
    • 0344756428 scopus 로고
    • On the structure of cardiolipin
    • J. LeCocq, and C.E. Ballou On the structure of cardiolipin Biochemistry 3 1964 976 980
    • (1964) Biochemistry , vol.3 , pp. 976-980
    • Lecocq, J.1    Ballou, C.E.2
  • 62
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • F.L. Hoch Cardiolipins and biomembrane function Biochim. Biophys. Acta 1113 1 1992 71 133
    • (1992) Biochim. Biophys. Acta , vol.1113 , Issue.1 , pp. 71-133
    • Hoch, F.L.1
  • 63
    • 0025831676 scopus 로고
    • Molecular species of cardiolipin in relation to other mitochondrial phospholipids. Is there an acyl specificity of the interaction between cardiolipin and the ADP/ATP carrier?
    • M. Schlame, K. Beyer, H. Hayer, and M. Klingenberg Molecular species of cardiolipin in relation to other mitochondrial phospholipids. Is there an acyl specificity of the interaction between cardiolipin and the ADP/ATP carrier? Eur. J. Biochem. 199 2 1991 459 466
    • (1991) Eur. J. Biochem. , vol.199 , Issue.2 , pp. 459-466
    • Schlame, M.1    Beyer, K.2    Hayer, H.3    Klingenberg, M.4
  • 64
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • M. Schlame, D. Rua, and M.L. Greenberg The biosynthesis and functional role of cardiolipin Prog. Lipid Res. 39 3 2000 257 288
    • (2000) Prog. Lipid Res. , vol.39 , Issue.3 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 65
    • 0034698098 scopus 로고    scopus 로고
    • Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function
    • F. Jiang, M.T. Ryan, M. Schlame, M. Zhao, Z. Gu, M. Klingenberg, N. Pfanner, and M.L. Greenberg Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function J. Biol. Chem. 275 29 2000 22387 22394
    • (2000) J. Biol. Chem. , vol.275 , Issue.29 , pp. 22387-22394
    • Jiang, F.1    Ryan, M.T.2    Schlame, M.3    Zhao, M.4    Gu, Z.5    Klingenberg, M.6    Pfanner, N.7    Greenberg, M.L.8
  • 66
    • 0029751960 scopus 로고    scopus 로고
    • Specific cardiolipin binding interferes with labeling of sulfhydryl residues in the adenosine diphosphate/adenosine triphosphate carrier protein from beef heart mitochondria
    • K. Beyer, and B. Nuscher Specific cardiolipin binding interferes with labeling of sulfhydryl residues in the adenosine diphosphate/adenosine triphosphate carrier protein from beef heart mitochondria Biochemistry 35 49 1996 15784 15790
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15784-15790
    • Beyer, K.1    Nuscher, B.2
  • 67
    • 0025172710 scopus 로고
    • Subunit analysis of bovine cytochrome c oxidase by reverse phase high performance liquid chromatography
    • N.C. Robinson, M.P. Dale, and L.H. Talbert Subunit analysis of bovine cytochrome c oxidase by reverse phase high performance liquid chromatography Arch. Biochem. Biophys. 281 2 1990 239 244
    • (1990) Arch. Biochem. Biophys. , vol.281 , Issue.2 , pp. 239-244
    • Robinson, N.C.1    Dale, M.P.2    Talbert, L.H.3
  • 68
    • 0027252494 scopus 로고
    • Functional binding of cardiolipin to cytochrome c oxidase
    • N.C. Robinson Functional binding of cardiolipin to cytochrome c oxidase J. Bioenerg. Biomembr. 25 2 1993 153 163
    • (1993) J. Bioenerg. Biomembr. , vol.25 , Issue.2 , pp. 153-163
    • Robinson, N.C.1
  • 69
    • 0033980879 scopus 로고    scopus 로고
    • X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides
    • K.E. McKAuley, P.K. Fyfe, R.J. Cogdell, N.W. Isaacs, and M.R. Jones X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides FEBS Lett. 467 2-3 2000 285 290
    • (2000) FEBS Lett. , vol.467 , Issue.23 , pp. 285-290
    • McKauley, K.E.1    Fyfe, P.K.2    Cogdell, R.J.3    Isaacs, N.W.4    Jones, M.R.5
  • 70
    • 0037143641 scopus 로고    scopus 로고
    • Interactions between lipids and bacterial reaction centers determined by protein crystallography
    • A. Camara-Artigas, D. Brune, and J.P. Allen Interactions between lipids and bacterial reaction centers determined by protein crystallography Proc. Natl. Acad. Sci. U. S. A. 99 17 2002 11055 11060
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.17 , pp. 11055-11060
    • Camara-Artigas, A.1    Brune, D.2    Allen, J.P.3
  • 72
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • M. Jormakka, S. Tornroth, B. Byrne, and S. Iwata Molecular basis of proton motive force generation: structure of formate dehydrogenase-N Science 295 5561 2002 1863 1868
    • (2002) Science , vol.295 , Issue.5561 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 74
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • E. Pebay-Peyroula, G. Dahout, R. Kahn, V. Trezeguet, G.J. Lauquin, and G. Brandolin Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside Nature 426 6962 2003 39 44
    • (2003) Nature , vol.426 , Issue.6962 , pp. 39-44
    • Pebay-Peyroula, E.1    Dahout, G.2    Kahn, R.3    Trezeguet, V.4    Lauquin, G.J.5    Brandolin, G.6
  • 75
    • 0042510861 scopus 로고    scopus 로고
    • Lipid-binding proteins: Structure of the phospholipid ligands
    • D. Marsh Lipid-binding proteins: structure of the phospholipid ligands Protein Sci. 12 9 2003 2109 2117
    • (2003) Protein Sci. , vol.12 , Issue.9 , pp. 2109-2117
    • Marsh, D.1
  • 76
    • 0042377402 scopus 로고    scopus 로고
    • Lipid interactions with transmembrane proteins
    • D. Marsh Lipid interactions with transmembrane proteins Cell Mol. Life Sci. 60 8 2003 1575 1580
    • (2003) Cell Mol. Life Sci. , vol.60 , Issue.8 , pp. 1575-1580
    • Marsh, D.1
  • 77
    • 0034732952 scopus 로고    scopus 로고
    • Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins
    • A.N. Ridder, S. Morein, J.G. Stam, A. Kuhn, B. de Kruijff, and J.A. Killian Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins Biochemistry 39 21 2000 6521 6528
    • (2000) Biochemistry , vol.39 , Issue.21 , pp. 6521-6528
    • Ridder, A.N.1    Morein, S.2    Stam, J.G.3    Kuhn, A.4    De Kruijff, B.5    Killian, J.A.6
  • 78
    • 0344497439 scopus 로고    scopus 로고
    • An atypical haem in the cytochrome b(6)f complex
    • D. Stroebel, Y. Choquet, J.L. Popot, and D. Picot An atypical haem in the cytochrome b(6)f complex Nature 426 6965 2003 413 418
    • (2003) Nature , vol.426 , Issue.6965 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.L.3    Picot, D.4
  • 79
    • 0242494128 scopus 로고    scopus 로고
    • 6f complex of oxygenic photosynthesis: Tuning the cavity
    • 6f complex of oxygenic photosynthesis: tuning the cavity Science 302 5647 2003 1009 1014
    • (2003) Science , vol.302 , Issue.5647 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 80
    • 0034724567 scopus 로고    scopus 로고
    • High-resolution structure of the OmpA membrane domain
    • A. Pautsch, and G.E. Schulz High-resolution structure of the OmpA membrane domain J. Mol. Biol. 298 2 2000 273 282
    • (2000) J. Mol. Biol. , vol.298 , Issue.2 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 82
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • A.D. Ferguson, E. Hofmann, J.W. Coulton, K. Diederichs, and W. Welte Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide Science 282 5397 1998 2215 2220
    • (1998) Science , vol.282 , Issue.5397 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 84
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • R. Vandeputte, R.A. Kramer, J. Kroon, N. Dekker, M.R. Egmond, and P. Gros Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site EMBO J. 20 18 2001 5033 5039
    • (2001) EMBO J. , vol.20 , Issue.18 , pp. 5033-5039
    • Vandeputte, R.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 85
    • 0037109010 scopus 로고    scopus 로고
    • Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy
    • C. Fernandez, C. Hilty, G. Wider, and K. Wuthrich Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 99 21 2002 13533 13537
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.21 , pp. 13533-13537
    • Fernandez, C.1    Hilty, C.2    Wider, G.3    Wuthrich, K.4
  • 86
    • 1642451819 scopus 로고    scopus 로고
    • Disruption of a specific molecular interaction with a bound lipid affects thermal stability of the purple bacterial reaction centre
    • P.K. Fyfe, N.W. Isaacs, R.J. Cogdell, and M.R. Jones Disruption of a specific molecular interaction with a bound lipid affects thermal stability of the purple bacterial reaction centre Biochim. Biophys. Acta 1608 1 2004 11 22
    • (2004) Biochim. Biophys. Acta , vol.1608 , Issue.1 , pp. 11-22
    • Fyfe, P.K.1    Isaacs, N.W.2    Cogdell, R.J.3    Jones, M.R.4
  • 88
    • 0035115358 scopus 로고    scopus 로고
    • Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?
    • M.C. Wakeham, R.B. Sessions, M.R. Jones, and P.K. Fyfe Is there a conserved interaction between cardiolipin and the type II bacterial reaction center? Biophys. J. 80 3 2001 1395 1405
    • (2001) Biophys. J. , vol.80 , Issue.3 , pp. 1395-1405
    • Wakeham, M.C.1    Sessions, R.B.2    Jones, M.R.3    Fyfe, P.K.4
  • 90
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • H. Schagger, and K. Pfeiffer Supercomplexes in the respiratory chains of yeast and mammalian mitochondria EMBO J. 19 8 2000 1777 1783
    • (2000) EMBO J. , vol.19 , Issue.8 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 91
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • H. Schagger Respiratory chain supercomplexes of mitochondria and bacteria Biochim. Biophys. Acta 1555 1-3 2002 154 159
    • (2002) Biochim. Biophys. Acta , vol.1555 , Issue.13 , pp. 154-159
    • Schagger, H.1
  • 92
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • M. Zhang, E. Mileykovskaya, and W. Dowhan Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane J. Biol. Chem. 277 46 2002 43553 43556
    • (2002) J. Biol. Chem. , vol.277 , Issue.46 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 94
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • C. Jungas, J.L. Ranck, J.L. Rigaud, P. Joliot, and A. Vermeglio Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides EMBO J. 18 3 1999 534 542
    • (1999) EMBO J. , vol.18 , Issue.3 , pp. 534-542
    • Jungas, C.1    Ranck, J.L.2    Rigaud, J.L.3    Joliot, P.4    Vermeglio, A.5
  • 95
    • 0037055974 scopus 로고    scopus 로고
    • Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria
    • A. Vermeglio, and P. Joliot Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria Biochim. Biophys. Acta 1555 1-3 2002 60 64
    • (2002) Biochim. Biophys. Acta , vol.1555 , Issue.13 , pp. 60-64
    • Vermeglio, A.1    Joliot, P.2
  • 97
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis Molscript: a program to produce both detailed and schematic plots of protein structures J. Appl.Cryst. 24 1991 946 950
    • (1991) J. Appl.Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 98
    • 0028057108 scopus 로고
    • Raster 3D Version 2.0. A program for photorealistic molecular graphics
    • E.A. Merritt, and M.E.P. Murphy Raster 3D Version 2.0. A program for photorealistic molecular graphics Acta Cryst. D. 50 1994 869 873
    • (1994) Acta Cryst. D. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 100
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 Pt 2 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , Issue.2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 101
    • 0034610266 scopus 로고    scopus 로고
    • Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
    • T. Nogi, I. Fathir, M. Kobayashi, T. Nozawa, and K. Miki Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer Proc. Natl. Acad. Sci. U. S. A. 97 25 2000 13561 13566
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.25 , pp. 13561-13566
    • Nogi, T.1    Fathir, I.2    Kobayashi, M.3    Nozawa, T.4    Miki, K.5
  • 102
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • A. Harrenga, and H. Michel The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction J. Biol. Chem. 274 47 1999 33296 33299
    • (1999) J. Biol. Chem. , vol.274 , Issue.47 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 103
    • 0043095535 scopus 로고    scopus 로고
    • Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution
    • G. Katona, U. Andreasson, E.M. Landau, L.E. Andreasson, and R. Neutze Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution J. Mol. Biol. 331 3 2003 681 692
    • (2003) J. Mol. Biol. , vol.331 , Issue.3 , pp. 681-692
    • Katona, G.1    Andreasson, U.2    Landau, E.M.3    Andreasson, L.E.4    Neutze, R.5


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