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Volumn 86, Issue 5, 2004, Pages 2837-2845

Structural Restraints and Heterogeneous Orientation of the Gramicidin A Channel Closed State in Lipid Bilayers

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GRAMICIDIN A;

EID: 0346127399     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74336-2     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 0026471029 scopus 로고
    • Molecular determinants of channel function
    • Andersen, O. S., and R. E. Koeppe, II. 1992. Molecular determinants of channel function. Physiol. Rev. 72:S89-S158.
    • (1992) Physiol. Rev. , vol.72
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 4
    • 0016172553 scopus 로고
    • Temperature-dependent properties of gramicidin A channels
    • Bamberg, E., and P. Lauger. 1974. Temperature-dependent properties of gramicidin A channels. Biochim. Biophys. Acta. 367:127-133.
    • (1974) Biochim. Biophys. Acta , vol.367 , pp. 127-133
    • Bamberg, E.1    Lauger, P.2
  • 6
    • 0032573081 scopus 로고    scopus 로고
    • The conducting form of gramicidin A is a right-handed double-stranded double helix
    • Burkhart, B. M., N. Li, D. A. Langs, W. A. Pangbom, and W. L. Duax. 1998. The conducting form of gramicidin A is a right-handed double-stranded double helix. Proc. Natl. Acad. Sci. USA. 95:12950-12955.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12950-12955
    • Burkhart, B.M.1    Li, N.2    Langs, D.A.3    Pangbom, W.A.4    Duax, W.L.5
  • 7
    • 0027533833 scopus 로고
    • The use of physical methods in determining gramicidin channel structure and function
    • Busath, D. D. 1993. The use of physical methods in determining gramicidin channel structure and function. Annu. Rev. Physiol. 55:473-501.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.D.1
  • 8
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. 3. Relationship between calcium adenosine triphosphatase enzyme activity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey, M., and G. W. Feigenson. 1981. Fluorescence quenching in model membranes. 3. Relationship between calcium adenosine triphosphatase enzyme activity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry. 20:1949-1961.
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 9
    • 0033019673 scopus 로고    scopus 로고
    • Solid state NMR and hydrogen-deuterium exchange of a bilayer solubilized peptide: Structural and mechanistic implications
    • Cotten, M., R. Fu, and T. A. Cross. 1999. Solid state NMR and hydrogen-deuterium exchange of a bilayer solubilized peptide: structural and mechanistic implications. Biophys. J. 76:1179-1189.
    • (1999) Biophys. J. , vol.76 , pp. 1179-1189
    • Cotten, M.1    Fu, R.2    Cross, T.A.3
  • 10
    • 0030748570 scopus 로고    scopus 로고
    • Protein stability and conformational rearrangements in lipid bilayers: Linear gramicidin, a model system
    • Cotten, M., F. Xu, and T. A. Cross. 1997. Protein stability and conformational rearrangements in lipid bilayers: linear gramicidin, a model system. Biophys. J. 73:614-623.
    • (1997) Biophys. J. , vol.73 , pp. 614-623
    • Cotten, M.1    Xu, F.2    Cross, T.A.3
  • 11
    • 0028025665 scopus 로고
    • Solid-state NMR structural studies of peptides and proteins in membranes
    • Cross, T. A., and S. J. Opella. 1994. Solid-state NMR structural studies of peptides and proteins in membranes. Curr. Opin. Struct. Biol. 4:574-581.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 12
    • 0037008040 scopus 로고    scopus 로고
    • The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane alpha-helical peptides depend on the nature of interfacially exposed aromatic and charged residues
    • de Planque, M. R., J. W. Boots, D. T. Rijkers, R. M. Liskamp, D. V. Greathouse, and J. A. Killian. 2002. The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane alpha-helical peptides depend on the nature of interfacially exposed aromatic and charged residues. Biochemistry. 41:8396-8404.
    • (2002) Biochemistry , vol.41 , pp. 8396-8404
    • De Planque, M.R.1    Boots, J.W.2    Rijkers, D.T.3    Liskamp, R.M.4    Greathouse, D.V.5    Killian, J.A.6
  • 13
    • 0031567125 scopus 로고    scopus 로고
    • Crystal structure of the gramicidin/ potassium thiocyanate complex
    • Doyle, D. A., and B. A. Wallace. 1997. Crystal structure of the gramicidin/ potassium thiocyanate complex. J. Mol. Biol. 266:963-977.
    • (1997) J. Mol. Biol. , vol.266 , pp. 963-977
    • Doyle, D.A.1    Wallace, B.A.2
  • 16
    • 0034000232 scopus 로고    scopus 로고
    • Inter- and intramolecular distance measurements by solid-state MAS NMR: Determination of gramicidin A channel dimer structure in hydrated phospholipid bilayers
    • Fu, R., M. Cotten, and T. A. Cross. 2000. Inter- and intramolecular distance measurements by solid-state MAS NMR: determination of gramicidin A channel dimer structure in hydrated phospholipid bilayers. J. Biomol. NMR. 16:261-268.
    • (2000) J. Biomol. NMR , vol.16 , pp. 261-268
    • Fu, R.1    Cotten, M.2    Cross, T.A.3
  • 17
    • 0032986388 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure
    • Fu, R., and T. A. Cross. 1999. Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure. Annu. Rev. Biophys. Biomol. Struct. 29:235-268.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 235-268
    • Fu, R.1    Cross, T.A.2
  • 18
    • 0033783447 scopus 로고    scopus 로고
    • 31P solid-state NMR spectruscopy investigation
    • 31P solid-state NMR spectruscopy investigation. Biochemistry. 39:13106-13114.
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 20
    • 0014969006 scopus 로고
    • Discreteness of conductance change in bimolecular lipid membranes in the presence of certain antibiotics
    • Hladky, S. B., and D. A. Haydon. 1970. Discreteness of conductance change in bimolecular lipid membranes in the presence of certain antibiotics. Nature. 5231:451-453.
    • (1970) Nature , vol.5231 , pp. 451-453
    • Hladky, S.B.1    Haydon, D.A.2
  • 21
    • 0015499206 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel
    • Hladky, S. B., and D. A. Haydon. 1972. Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochim. Biophys. Acta. 274:294-312.
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 22
    • 0000039285 scopus 로고
    • Ion movement in gramicidin channels
    • F. Bronner and W. D. Stein, editors. Academic Press, San Diego
    • Hladky, S. B., and D. A. Haydon. 1984. Ion movement in gramicidin channels. In Current Topics in Membranes and Transport, Vol. 21. F. Bronner and W. D. Stein, editors. Academic Press, San Diego.
    • (1984) Current Topics in Membranes and Transport , vol.21
    • Hladky, S.B.1    Haydon, D.A.2
  • 23
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channel
    • Hu, W., N. D. Lazo, and T. A. Cross. 1995. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channel. Biochemistry. 34:14138-14146.
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.D.2    Cross, T.A.3
  • 24
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid-bilayer by solid-state NMR
    • Ketchem, R. R., W. Hu, and T. A. Cross. 1993. High-resolution conformation of gramicidin A in a lipid-bilayer by solid-state NMR. Science. 261:1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 25
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints
    • Ketchem, R. R., B. Roux, and T. A. Cross. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints. Structure. 5:1655-1669.
    • (1997) Structure , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 26
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian, J. A., I. Salemink, M. R. de Planque, G. Lindblom, R. E. Koeppe II, and D. V. Greathouse. 1996. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 35:1037-1045.
    • (1996) Biochemistry , vol.35 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    De Planque, M.R.3    Lindblom, G.4    Koeppe II, R.E.5    Greathouse, D.V.6
  • 27
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. 1988. Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science. 241:188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 28
    • 0026079920 scopus 로고
    • Monoclinic uncomplexed double-stranded, antiparallel, left-handed beta 5.6-helix structure of gramicidin A
    • Langs, D. A., G. D. Smith, C. Courseille, G. Precigoux, and M. Hospital. 1991. Monoclinic uncomplexed double-stranded, antiparallel, left-handed beta 5.6-helix structure of gramicidin A. Proc. Natl. Acad. Sci. USA. 88:5345-5349.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5345-5349
    • Langs, D.A.1    Smith, G.D.2    Courseille, C.3    Precigoux, G.4    Hospital, M.5
  • 29
    • 0027716064 scopus 로고
    • Rapidly-frozen polypeptide samples for characterization of high definition dynamics by solid-state NMR spectroscopy
    • Lazo, N. D., W. Hu, K.-C. Lee, and T. A. Cross. 1993. Rapidly-frozen polypeptide samples for characterization of high definition dynamics by solid-state NMR spectroscopy. Biochem. Biophys. Res. Commun. 197:904-909.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 904-909
    • Lazo, N.D.1    Hu, W.2    Lee, K.-C.3    Cross, T.A.4
  • 30
    • 0027329868 scopus 로고
    • 2H NMR determination of the global correlation time of the gramicidin channel in a lipid bilayer
    • 2H NMR determination of the global correlation time of the gramicidin channel in a lipid bilayer. Biophys. J. 65:1162-1167.
    • (1993) Biophys. J. , vol.65 , pp. 1162-1167
    • Lee, K.-C.1    Hu, W.2    Cross, T.A.3
  • 31
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis, B. A., and D. M. Engelman. 1983. Lipid bilayer thickness varies with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166:211-217.
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 32
    • 0026813599 scopus 로고
    • Refinement of the spatial structure of the gramicidin A ion channel
    • Russian
    • Lomize, A. L., V. Orekhov, and A. S. Arsen'ev. 1992. Refinement of the spatial structure of the gramicidin A ion channel. Bioorg. Khim. 18:182-200. (Russian).
    • (1992) Bioorg. Khim. , vol.18 , pp. 182-200
    • Lomize, A.L.1    Orekhov, V.2    Arsen'ev, A.S.3
  • 33
    • 0027503130 scopus 로고
    • Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: The polypeptide backbone of gramicidin A in a lipid bilayer
    • Mai, W., W. Hu, C. Wang, and T. A. Cross. 1993. Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: the polypeptide backbone of gramicidin A in a lipid bilayer. Protein Sci. 2:532-542.
    • (1993) Protein Sci. , vol.2 , pp. 532-542
    • Mai, W.1    Hu, W.2    Wang, C.3    Cross, T.A.4
  • 34
    • 0037007145 scopus 로고    scopus 로고
    • Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness
    • Martinac, B., and O. P. Hamill. 2001. Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness. Proc. Natl. Acad. Sci. USA. 99:4308-4312.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4308-4312
    • Martinac, B.1    Hamill, O.P.2
  • 35
    • 0030827053 scopus 로고    scopus 로고
    • Water accessibility to the tryptophan indole N-H sites of gramicidin A transmembrane channel: Detection of positional shifts of tryptophans 11 and 13 along the channel axis upon cation binding
    • Maruyama, T., and H. Takeuchi. 1997. Water accessibility to the tryptophan indole N-H sites of gramicidin A transmembrane channel: detection of positional shifts of tryptophans 11 and 13 along the channel axis upon cation binding. Biochemistry. 36:10993-11001.
    • (1997) Biochemistry , vol.36 , pp. 10993-11001
    • Maruyama, T.1    Takeuchi, H.2
  • 36
    • 0024577141 scopus 로고
    • The different influences of ether and ester phospholipids on the conformation of gramicidin A. A molecular modelling study
    • Meulendijks, G. H., W. M. Sonderkamp, J. E. Dubois, R. J. Nielen, J. A. Kremers, and H. M. Buck. 1989. The different influences of ether and ester phospholipids on the conformation of gramicidin A. A molecular modelling study. Biochim. Biophys. Acta. 979:321-330.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 321-330
    • Meulendijks, G.H.1    Sonderkamp, W.M.2    Dubois, J.E.3    Nielen, R.J.4    Kremers, J.A.5    Buck, H.M.6
  • 37
    • 0030758516 scopus 로고    scopus 로고
    • The conformational preference of gramicidin channels is a function of lipid bilayer thickness
    • Mobashery, N., C. Nielsen, and O. S. Andersen. 1997. The conformational preference of gramicidin channels is a function of lipid bilayer thickness. FEBS Lett. 412:15-20.
    • (1997) FEBS Lett. , vol.412 , pp. 15-20
    • Mobashery, N.1    Nielsen, C.2    Andersen, O.S.3
  • 39
    • 0025667349 scopus 로고
    • Kinetics of gramicidin channel formation in lipid bilayers: Transmembrane monomer association
    • O'Connell, A. M., R. E. Koeppe II, and O. S. Andersen. 1990. Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association. Science. 250:1256-1259.
    • (1990) Science , vol.250 , pp. 1256-1259
    • O'Connell, A.M.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 40
    • 0026480686 scopus 로고
    • Structure of an isolated gramicidin A double helical species by high resolution nuclear magnetic resonance
    • Pascal, S. M., and T. A. Cross. 1992. Structure of an isolated gramicidin A double helical species by high resolution nuclear magnetic resonance. J. Mol. Biol. 226:1101-1109.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1101-1109
    • Pascal, S.M.1    Cross, T.A.2
  • 41
    • 0027666089 scopus 로고
    • High-resolution structure and dynamic implications for a double-helical gramicidin A conformer
    • Pascal, S. M., and T. A. Cross. 1993. High-resolution structure and dynamic implications for a double-helical gramicidin A conformer. J. Biomol. NMR. 3:495-513.
    • (1993) J. Biomol. NMR , vol.3 , pp. 495-513
    • Pascal, S.M.1    Cross, T.A.2
  • 42
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 43
    • 0024281616 scopus 로고
    • Structural polymorphism in transmembrane channels
    • Salemme, F. R. 1988. Structural polymorphism in transmembrane channels. Science. 241:145, 230.
    • (1988) Science , vol.241 , pp. 145
    • Salemme, F.R.1
  • 44
    • 0028916495 scopus 로고
    • HPLC demonstration that an all trp→phe replacement in gramicidin A results in a conformational rearrangement from β-helical monomer to double-stranded dimer in model membranes
    • Salom, D., M. C. Bañó, L. Braco, and C. Abad. 1995. HPLC demonstration that an all trp→phe replacement in gramicidin A results in a conformational rearrangement from β-helical monomer to double-stranded dimer in model membranes. Biochem. Biophys. Res. Commun. 209:446-473.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 446-473
    • Salom, D.1    Bañó, M.C.2    Braco, L.3    Abad, C.4
  • 45
    • 0026051563 scopus 로고
    • Effect of increased chain packing on gramicidin-lipid interactions
    • Scarlata, S. F. 1991. Effect of increased chain packing on gramicidin-lipid interactions. Biochemistry. 30:9853-9859.
    • (1991) Biochemistry , vol.30 , pp. 9853-9859
    • Scarlata, S.F.1
  • 46
    • 0344522332 scopus 로고
    • 13C nuclear magnetic resonance study
    • 13C nuclear magnetic resonance study. Biophys. J. 49:117-118.
    • (1986) Biophys. J. , vol.49 , pp. 117-118
    • Smith, R.1    Cornell, B.A.2
  • 47
    • 0001164631 scopus 로고
    • 15N chemical-shift tensor orientation in a polypeptide
    • 15N chemical-shift tensor orientation in a polypeptide. J. Magn. Reson. 85:439-447.
    • (1989) J. Magn. Reson. , vol.85 , pp. 439-447
    • Teng, Q.1    Cross, T.A.2
  • 48
    • 0035797933 scopus 로고    scopus 로고
    • Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles
    • Townsley, L. E., W. A. Tucker, S. Sham, and J. F. Hinton. 2001. Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. Biochemistry. 40:11676-11686.
    • (2001) Biochemistry , vol.40 , pp. 11676-11686
    • Townsley, L.E.1    Tucker, W.A.2    Sham, S.3    Hinton, J.F.4
  • 49
    • 0016776797 scopus 로고
    • Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of Gramicidin A
    • Veatch, W. R., R. Mathies, M. Eisenberg, and L. Stryer. 1975. Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of Gramicidin A. J. Mol. Biol. 90:75-92.
    • (1975) J. Mol. Biol. , vol.90 , pp. 75-92
    • Veatch, W.R.1    Mathies, R.2    Eisenberg, M.3    Stryer, L.4
  • 50
    • 0024281633 scopus 로고
    • The gramicidin pore: Crystal structure of a cesium complex
    • Wallace, B. A., and K. Ravikumar. 1988. The gramicidin pore: crystal structure of a cesium complex. Science. 241:182-187.
    • (1988) Science , vol.241 , pp. 182-187
    • Wallace, B.A.1    Ravikumar, K.2
  • 51
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphos-phatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • Wiener, M. C., and S. H. White. 1992. Structure of a fluid dioleoylphos-phatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61:437-447.
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, M.C.1    White, S.H.2
  • 52
    • 0033529783 scopus 로고    scopus 로고
    • Water: Foldase activity in catalyzing polypeptide conformational rearrangements
    • Xu, F., and T. A. Cross. 1999. Water: foldase activity in catalyzing polypeptide conformational rearrangements. Proc. Natl. Acad. Sci. USA. 96:9057-9061.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9057-9061
    • Xu, F.1    Cross, T.A.2
  • 53
    • 0029807213 scopus 로고    scopus 로고
    • A catalytic role for protic solvents in conformational interconversion
    • Xu, F., A. Wang, J. B. Vaughn, and T. A. Cross. 1996. A catalytic role for protic solvents in conformational interconversion. J. Am. Chem. Soc. 118:9176-9177.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9176-9177
    • Xu, F.1    Wang, A.2    Vaughn, J.B.3    Cross, T.A.4


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