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Volumn 120, Issue 2, 2003, Pages 93-102

Microscopic assessment of membrane protein structure and function

Author keywords

3D electron microscopy; Atomic force microscopy; Electron diffraction; Membrane protein crystallization

Indexed keywords

AQUAPORIN; MEMBRANE PROTEIN; PORIN; RHODOPSIN; OUTER MEMBRANE PROTEIN;

EID: 0042329979     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00418-003-0560-1     Document Type: Conference Paper
Times cited : (12)

References (68)
  • 2
    • 0036828872 scopus 로고    scopus 로고
    • pH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding
    • Andersen C, Schiffier B, Charbit A, Benz R (2002) pH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J Biol Chem 277:41318-41325
    • (2002) J Biol Chem , vol.277 , pp. 41318-41325
    • Andersen, C.1    Schiffier, B.2    Charbit, A.3    Benz, R.4
  • 3
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans
    • Baumeister W, Barth M, Hegerl R, Guckenberger R, Hahn M, Saxton WO (1986) Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans. J Mol Biol 187:241-253
    • (1986) J Mol Biol , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 4
    • 0035900750 scopus 로고    scopus 로고
    • Three-dimensional model and characterization of the iron stress-induced CP43′-photosystem I supercomplex isolated from the cyanobacterium Synechocystis PCC 6803
    • Bibby TS, Nield J, Barber J (2001) Three-dimensional model and characterization of the iron stress-induced CP43′-photosystem I supercomplex isolated from the cyanobacterium Synechocystis PCC 6803. J Biol Chem 276:43246-43252
    • (2001) J Biol Chem , vol.276 , pp. 43246-43252
    • Bibby, T.S.1    Nield, J.2    Barber, J.3
  • 6
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton C, Haase W, Rapoport TA, Kühlbrandt W, Collinson I (2002) Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 418:662-665
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.5
  • 7
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220-2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 11
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot BL, Grubmüller H (2001) Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science 294:2353-2357
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmüller, H.2
  • 12
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • de Groot BL, Engel A, Grubmüller H (2001) A refined structure of human aquaporin-1. FEBS Lett 504:206-211
    • (2001) FEBS Lett , vol.504 , pp. 206-211
    • De Groot, B.L.1    Engel, A.2    Grubmüller, H.3
  • 13
    • 0037227425 scopus 로고    scopus 로고
    • The structure of the aquaporin-1 water channel: A comparison between cryo-electron microscopy and X-ray crystallography
    • de Groot B, Engel A, Grubmüller H (2003) The structure of the aquaporin-1 water channel: a comparison between cryo-electron microscopy and X-ray crystallography. J Mol Biol 325:485-493
    • (2003) J Mol Biol , vol.325 , pp. 485-493
    • De Groot, B.1    Engel, A.2    Grubmüller, H.3
  • 16
    • 0022380710 scopus 로고
    • Porin channel triplets merge into single outlets in Escherichia coli outer membranes
    • Engel A, Massalski A, Schindler H, Dorset DL, Rosenbusch JP (1985) Porin channel triplets merge into single outlets in Escherichia coli outer membranes. Nature 317:643-645
    • (1985) Nature , vol.317 , pp. 643-645
    • Engel, A.1    Massalski, A.2    Schindler, H.3    Dorset, D.L.4    Rosenbusch, J.P.5
  • 17
    • 0035979788 scopus 로고    scopus 로고
    • Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli
    • Fernandez C, Hilty C, Bonjour S, Adeishvili K, Pervushin K, Wuthrich K (2001) Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli. FEBS Lett 504:173-178
    • (2001) FEBS Lett , vol.504 , pp. 173-178
    • Fernandez, C.1    Hilty, C.2    Bonjour, S.3    Adeishvili, K.4    Pervushin, K.5    Wuthrich, K.6
  • 19
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher TE, Marszalek PE, Fernandez JM (2000) Stretching single molecules into novel conformations using the atomic force microscope. Nat Struct Biol 7:719-724
    • (2000) Nat Struct Biol , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 24
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank J (2002) Single-particle imaging of macromolecules by cryo-electron microscopy. Annu Rev Biophys Biomol Struct 31:303-319
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 303-319
    • Frank, J.1
  • 26
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi Y (1998) The structural study of membrane proteins by electron crystallography. Adv Biophys 35:25-80
    • (1998) Adv Biophys , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 27
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff N (1998) Three-dimensional structure of bovine NADH: ubiquinone oxidoreductase (complex I) at 22 Å in ice. J Mol Biol 277:1033-1046
    • (1998) J Mol Biol , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 29
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213:899-929
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 30
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: Application to structural study on bacteriorhodopsin
    • Hirai T, Murata K, Kimura Y, Fujiyoshi Y (1999) Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin. J Electron Microsc 48:653-685
    • (1999) J Electron Microsc , vol.48 , pp. 653-685
    • Hirai, T.1    Murata, K.2    Kimura, Y.3    Fujiyoshi, Y.4
  • 34
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W, Wang DN, Fujiyoshi Y (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367:614-621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 35
    • 0035979759 scopus 로고    scopus 로고
    • Succinate:quinone oxidoreductases: What can we learn from Wolinella succinogenes quinol:fumarate reductase?
    • Lancaster CR (2001) Succinate:quinone oxidoreductases: what can we learn from Wolinella succinogenes quinol:fumarate reductase? FEBS Lett 504:133-141
    • (2001) FEBS Lett , vol.504 , pp. 133-141
    • Lancaster, C.R.1
  • 36
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y, Fotiadis D, Filipek S, Saperstein DA, Palczewski K, Engel A (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J Biol Chem 278:21655-21662
    • (2003) J Biol Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 37
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296:1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 39
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O, Weber I, Frangakis AS, Nicastro D, Gerisch G, Baumeister W (2002) Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 298:1209-1213
    • (2002) Science , vol.298 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 40
    • 0035843079 scopus 로고    scopus 로고
    • Projection structure of a ClC-type chloride channel at 6.5 Å resolution
    • Mindell JA, Maduke M, Miller C, Grigorieff N (2001) Projection structure of a ClC-type chloride channel at 6.5 Å resolution. Nature 409:219-223
    • (2001) Nature , vol.409 , pp. 219-223
    • Mindell, J.A.1    Maduke, M.2    Miller, C.3    Grigorieff, N.4
  • 41
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka K, Hirai T, Murata K, Miyazawa A, Kidera A, Kimura Y, Fujiyoshi Y (1999a) The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J Mol Biol 286:861-882
    • (1999) J Mol Biol , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 43
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller DJ, Engel A (1999) Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J Mol Biol 285:1347-1351
    • (1999) J Mol Biol , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 44
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy
    • Müller DJ, Baumeister W, Engel A (1996) Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy. J Bacteriol 178:3025-3030
    • (1996) J Bacteriol , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 45
    • 0033539578 scopus 로고    scopus 로고
    • Controlled unzipping of a bacterial surface layer with an AFM
    • Müller DJ, Baumeister W, Engel A (1999a) Controlled unzipping of a bacterial surface layer with an AFM. Proc Natl Acad Sci U S A 96:13170-13174
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13170-13174
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 46
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • Müller DJ, Fotiadis D, Scheuring S, Müller SA, Engel A (1999b) Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope. Biophys J 76:1101-1111
    • (1999) Biophys J , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 49
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 ångstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM (1997) X-ray structure of bacteriorhodopsin at 2.5 ångstroms from microcrystals grown in lipidic cubic phases. Science 277:1676-1681
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 50
    • 0023448994 scopus 로고
    • Nucleotide sequence of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies
    • Peters J, Peters M, Lottspeich F, Schäfer W, Baumeister W (1987) Nucleotide sequence of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies. J Bacteriol 169:5216-5223
    • (1987) J Bacteriol , vol.169 , pp. 5216-5223
    • Peters, J.1    Peters, M.2    Lottspeich, F.3    Schäfer, W.4    Baumeister, W.5
  • 51
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385-387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 52
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA (2001) G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol Ther 92:71-87
    • (2001) Pharmacol Ther , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 54
  • 55
    • 0036094131 scopus 로고    scopus 로고
    • Charting and unzipping the surface layer of Corynebacterium glutamicum with the atomic force microscope
    • Scheuring S, Stahlberg H, Chami M, Houssin C, Rigaud JL, Engel A (2002b) Charting and unzipping the surface layer of Corynebacterium glutamicum with the atomic force microscope. Mol Microbiol 44:675-684
    • (2002) Mol Microbiol , vol.44 , pp. 675-684
    • Scheuring, S.1    Stahlberg, H.2    Chami, M.3    Houssin, C.4    Rigaud, J.L.5    Engel, A.6
  • 56
    • 0010457541 scopus 로고
    • Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers
    • Schindler H, Rosenbusch JP (1978) Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc Natl Acad Sci U S A 75:3751-3755
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3751-3755
    • Schindler, H.1    Rosenbusch, J.P.2
  • 57
    • 0033579482 scopus 로고    scopus 로고
    • Brownian dynamics simulation of ion flow through porin channels
    • Schirmer T, Phale PS (1999) Brownian dynamics simulation of ion flow through porin channels. J Mol Biol 294:1159-1167
    • (1999) J Mol Biol , vol.294 , pp. 1159-1167
    • Schirmer, T.1    Phale, P.S.2
  • 59
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: An overview
    • Sleytr UB (1997) Basic and applied S-layer research: an overview. FEMS Microbiol Rev 20:5-12
    • (1997) FEMS Microbiol Rev , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 63
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H, Han BG, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 66
    • 0028175266 scopus 로고
    • Biologically active 2-dimensional crystals of aquaporin CHIP
    • Walz T, Smith BL, Zeidel ML, Engel A, Agre P (1994) Biologically active 2-dimensional crystals of aquaporin CHIP. J Biol Chem 269:1583-1586
    • (1994) J Biol Chem , vol.269 , pp. 1583-1586
    • Walz, T.1    Smith, B.L.2    Zeidel, M.L.3    Engel, A.4    Agre, P.5
  • 68
    • 0034610788 scopus 로고    scopus 로고
    • Three-dimensional structure of the ion-coupled transport protein NhaA
    • Williams KA (2000) Three-dimensional structure of the ion-coupled transport protein NhaA. Nature 403:112-115
    • (2000) Nature , vol.403 , pp. 112-115
    • Williams, K.A.1


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