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Volumn 264, Issue 4, 1996, Pages 757-769

Solution structure of a parallel left-handed double-helical gramicidin-A determined by 2D 1H NMR

Author keywords

Antibiotic structure; Calcium binding; Membrane polypeptide; Nuclear magnetic resonance

Indexed keywords

ANTIBIOTIC AGENT; CALCIUM ION; GRAMICIDIN A;

EID: 0030582738     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0675     Document Type: Article
Times cited : (38)

References (36)
  • 3
    • 0020475305 scopus 로고
    • 1H-nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations
    • 1H-nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. J. Mol. Biol. 155, 321-346.
    • (1982) J. Mol. Biol. , vol.155 , pp. 321-346
    • Billeter, M.1    Braun, W.2    Wuthrich, K.3
  • 4
    • 0022885390 scopus 로고
    • DNA-supercoiling is affected in vitro by the peptide antibiotics tyrocidine and gramicidin
    • Bohg, A. & Ristow, H. (1986). DNA-supercoiling is affected in vitro by the peptide antibiotics tyrocidine and gramicidin. European J. Biochem. 160, 587-591.
    • (1986) European J. Biochem. , vol.160 , pp. 587-591
    • Bohg, A.1    Ristow, H.2
  • 7
    • 0011262383 scopus 로고
    • The structure of the transmembrane channel of gramicidin A: NMR study of its conformational stability and interaction with divalent cations
    • Bystrov, V. F., Arseniev, A. S., Barsukov, V. I., Golovanov, A. P. & Maslennikikov, I. V. (1990). The structure of the transmembrane channel of gramicidin A: NMR study of its conformational stability and interaction with divalent cations. Gazz. Chim. Ital. 120, 485-491.
    • (1990) Gazz. Chim. Ital. , vol.120 , pp. 485-491
    • Bystrov, V.F.1    Arseniev, A.S.2    Barsukov, V.I.3    Golovanov, A.P.4    Maslennikikov, I.V.5
  • 8
    • 0001546676 scopus 로고
    • Fractionation of bactericidal agent from cultures of a soil bacillus
    • Hotchkiss, R. D. & Dubos, R. J. (1940). Fractionation of bactericidal agent from cultures of a soil bacillus. J. Biol. Chem. 132, 791-792.
    • (1940) J. Biol. Chem. , vol.132 , pp. 791-792
    • Hotchkiss, R.D.1    Dubos, R.J.2
  • 9
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
    • Hu, W., Lee, K. C. & Cross, T. A. (1993). Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel. Biochemistry, 32, 7035-7047.
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.C.2    Cross, T.A.3
  • 10
    • 33745356391 scopus 로고
    • Contact electron-spin interaction of nuclear magnetic moment
    • Karplus, M. (1959). Contact electron-spin interaction of nuclear magnetic moment. J. Phys. Chem. 30, 11-15.
    • (1959) J. Phys. Chem. , vol.30 , pp. 11-15
    • Karplus, M.1
  • 11
    • 0001053688 scopus 로고
    • A theoretical study of distance determinations from NMR 2 dimensional nuclear overhauser effect spectra
    • Keepers, J. W. & James, T. L. (1984). A theoretical study of distance determinations from NMR 2 dimensional nuclear overhauser effect spectra. J. Magn. Reson. 57, 404-426.
    • (1984) J. Magn. Reson. , vol.57 , pp. 404-426
    • Keepers, J.W.1    James, T.L.2
  • 12
    • 0027360175 scopus 로고
    • High resolution conformation of gramicidin A in a lipid bilayer by solid state NMR
    • Ketchem, R. R., Hu, W. & Cross, T. A. (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
  • 13
    • 0028045061 scopus 로고
    • Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
    • Koeppe, R. E., II, Killian, J. A. & Greathouse, D. V. (1994). Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J. 66, 14-24.
    • (1994) Biophys. J. , vol.66 , pp. 14-24
    • Koeppe R.E. II1    Killian, J.A.2    Greathouse, D.V.3
  • 14
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 A of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. (1988). Three-dimensional structure at 0.86 A 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
  • 15
    • 0026079920 scopus 로고
    • Monoclinic uncomplexed double-stranded, antiparallel, left-handed β-5.6-helix (↑↓β-5.6) structure of gramicidin-A. Alternate patterns of helical association and deformation
    • Langs, D. A., Smith, G. D., Courseille, C., Precigoux, G. & Hospital, M. (1991). Monoclinic uncomplexed double-stranded, antiparallel, left-handed β-5.6-helix (↑↓β-5.6) structure of gramicidin-A. Alternate patterns of helical association and deformation. 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
  • 16
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. & Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 17
    • 0027999315 scopus 로고
    • Knowledge-based validation of protein structure coordinates derived by X-ray crystallography and NMR spectroscopy
    • MacArthur, M. W., Laskowski, R. A. & Thornton, J. M. (1994). Knowledge-based validation of protein structure coordinates derived by X-ray crystallography and NMR spectroscopy. Curr. Opin. Struct. Biol. 4, 731-737.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 731-737
    • MacArthur, M.W.1    Laskowski, R.A.2    Thornton, J.M.3
  • 18
    • 84986435971 scopus 로고
    • The nature of the N-H O = C hydrogen-bond. An intermolecular perturbation theory study of the formamide formaldehyde complex
    • Mitchell, J. B. O. & Price, S. L. (1990). The nature of the N-H O = C hydrogen-bond. An intermolecular perturbation theory study of the formamide formaldehyde complex. J. Comput. Chem. 11, 1217-1233.
    • (1990) J. Comput. Chem. , vol.11 , pp. 1217-1233
    • Mitchell, J.B.O.1    Price, S.L.2
  • 19
    • 0023732144 scopus 로고
    • Determination of 3-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges, M., Clore, G. M. & Gronenborn, A. M. (1988). Determination of 3-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Letters, 239, 129-136.
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 20
    • 0000732609 scopus 로고
    • GRASP-graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP-graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 21
    • 0026480686 scopus 로고
    • Structure of an isolated gramicidin A double helical species by high resolution nuclear magnetic resonance
    • Pascal, S. M. & Cross, T. A. (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
  • 22
    • 0027666089 scopus 로고
    • High resolution structure and dynamic implications for a double-helical gramicidin A conformer
    • Pascal, S. M. & Cross, T. A. (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
  • 23
    • 0018671469 scopus 로고
    • Comparison of the effect of linear gramicidin analogues on bacterial sporulation, membrane permeability, and ribonucleic acid polymerase
    • Paulus, H., Sarkar, N., Mukherjee, P. K., Langley, D., Ivanov, V. T., Shepel, E. N. & Veatch W. (1979). Comparison of the effect of linear gramicidin analogues on bacterial sporulation, membrane permeability, and ribonucleic acid polymerase. Biochemistry, 18, 4532-4536.
    • (1979) Biochemistry , vol.18 , pp. 4532-4536
    • Paulus, H.1    Sarkar, N.2    Mukherjee, P.K.3    Langley, D.4    Ivanov, V.T.5    Shepel, E.N.6    Veatch, W.7
  • 24
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous-solutions
    • Piotto, M., Saudek, V. & Skeenár, V. (1992). Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous-solutions. J. Biomol. NMR, 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Skeenár, V.3
  • 25
    • 33947482744 scopus 로고
    • Gramicidin A. V. The structure of valine- and isoleucine-gramicidin A
    • Sarges, R. & Witkop, B. (1965). Gramicidin A. V. The structure of valine- and isoleucine-gramicidin A. J. Am. Chem. Soc. 87, 2011-2020.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2011-2020
    • Sarges, R.1    Witkop, B.2
  • 27
    • 0027519324 scopus 로고
    • The double π-π-5.6 helix of gramicidin A predominates in unsaturated lipid membranes
    • Sychev, S. V., Barsukov, L. I. & Ivanov, V. T. (1993). The double π-π-5.6 helix of gramicidin A predominates in unsaturated lipid membranes. Eur. Biophys. J. 22, 279-298.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 279-298
    • Sychev, S.V.1    Barsukov, L.I.2    Ivanov, V.T.3
  • 28
    • 0025103378 scopus 로고
    • Environments and conformations of tryptophans side chains of gramicidin A in phospholipid bilayers studied by Raman spectroscopy
    • Takeuchi, H., Nemoto, Y. & Harada, I. (1990). Environments and conformations of tryptophans side chains of gramicidin A in phospholipid bilayers studied by Raman spectroscopy. Biochemistry, 29, 1572-1579.
    • (1990) Biochemistry , vol.29 , pp. 1572-1579
    • Takeuchi, H.1    Nemoto, Y.2    Harada, I.3
  • 29
    • 0015027073 scopus 로고
    • The gramicidin A transmembrane channel: A proposed π(L,D) helix
    • Urry, D. W. (1972). The gramicidin A transmembrane channel: a proposed π(L,D) helix. Proc. Natl Acad. Sci. USA, 68, 672-676.
    • (1972) Proc. Natl Acad. Sci. USA , vol.68 , pp. 672-676
    • Urry, D.W.1
  • 30
    • 0016290374 scopus 로고
    • The conformation of gramicidin A
    • Veatch, W. R., Fossel, E. T. & Blout, E. R. (1974). The conformation of gramicidin A. Biochemistry, 13, 5249-5256.
    • (1974) Biochemistry , vol.13 , pp. 5249-5256
    • Veatch, W.R.1    Fossel, E.T.2    Blout, E.R.3
  • 31
    • 0024281633 scopus 로고
    • The gramicidin pore: Crystal structure of a cesium complex
    • Wallace, B. A. & Ravikumar, K. (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
  • 32
    • 0019852927 scopus 로고
    • Conformation of gramicidin A in phospholipid vesicles: Circular dichroism studies of effects of ion binding, chemical modification, and lipid structure
    • Wallace, B. A., Veatch, W. R. & Blout, E. R. (1981). Conformation of gramicidin A in phospholipid vesicles: circular dichroism studies of effects of ion binding, chemical modification, and lipid structure. Biochemistry, 20, 5754-5760.
    • (1981) Biochemistry , vol.20 , pp. 5754-5760
    • Wallace, B.A.1    Veatch, W.R.2    Blout, E.R.3
  • 33
    • 0026499150 scopus 로고
    • Gramicidin-lipid interactions induce specific tryptophan side chain conformations
    • Woolley, G. A., Dunn, A. & Wallace, B. A. (1992). Gramicidin-lipid interactions induce specific tryptophan side chain conformations. Biochem. Soc. Trans. 20, 864-867.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 864-867
    • Woolley, G.A.1    Dunn, A.2    Wallace, B.A.3
  • 35
    • 0028823379 scopus 로고
    • The conformation of an alamethicin in methanol by multinuclear NMR spectrosocopy and distance geometry/simulated annealing
    • Yee, A. A., Babiuk, R. & O'Neil, J. D. J. (1995). The conformation of an alamethicin in methanol by multinuclear NMR spectrosocopy and distance geometry/simulated annealing. Biopolymers, 36, 781-792.
    • (1995) Biopolymers , vol.36 , pp. 781-792
    • Yee, A.A.1    Babiuk, R.2    O'Neil, J.D.J.3
  • 36
    • 0026738754 scopus 로고
    • A conformational rearrangement in gramicidin A. From a double-stranded left-handed to a single-stranded right-handed helix
    • Zhang, Z. L., Pascal, S. M. & Cross, T. A. (1992). A conformational rearrangement in gramicidin A. From a double-stranded left-handed to a single-stranded right-handed helix. Biochemistry, 31, 8822-8828.
    • (1992) Biochemistry , vol.31 , pp. 8822-8828
    • Zhang, Z.L.1    Pascal, S.M.2    Cross, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.