메뉴 건너뛰기




Volumn 43, Issue 44, 2004, Pages 13972-13980

Membrane assembly of M13 major coat protein: Evidence for a structural adaptation in the hinge region and a tilted transmembrane domain

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; COMPOSITION; CONFORMATIONS; ENVIRONMENTAL IMPACT; ENZYMES; FLUORESCENCE; HYDROPHILICITY; MOLECULAR STRUCTURE;

EID: 8344287531     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048437x     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin, D. A. (1998) Filamentous phage structure, infection and assembly, Curr. Opin. Struct. Biol. 8, 150-158.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 3
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. (2003) Lipid-protein interactions in biological membranes: a structural perspective, Biochim. Biophys. Acta 1612, 1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 4
    • 0031577283 scopus 로고    scopus 로고
    • Fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • Almeida, F. C. L., and Opella, S. J. (1997) Fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix, J. Mol. Biol. 270, 481-495.
    • (1997) J. Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.L.1    Opella, S.J.2
  • 5
    • 0032544545 scopus 로고    scopus 로고
    • Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues
    • Papavoine, C. H. M., Christiaans, B. E. C., Folmer, R. H. A., Konings, R. N. H., and Hilbers, C. W. (1998) Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues, J. Mol. Biol. 252, 401-419.
    • (1998) J. Mol. Biol. , vol.252 , pp. 401-419
    • Papavoine, C.H.M.1    Christiaans, B.E.C.2    Folmer, R.H.A.3    Konings, R.N.H.4    Hilbers, C.W.5
  • 6
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi, F. M., and Opella, S. J. (2003) Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints, Protein Sci. 12, 403-411.
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 7
    • 0027438626 scopus 로고
    • Fd coat protein structure in membrane environments
    • McDonnell, P. A., Shon, K., Kim, Y., and Opella, S. J. (1993) Fd coat protein structure in membrane environments, J. Mol. Biol. 233, 447-463.
    • (1993) J. Mol. Biol. , vol.233 , pp. 447-463
    • McDonnell, P.A.1    Shon, K.2    Kim, Y.3    Opella, S.J.4
  • 9
    • 0030787637 scopus 로고    scopus 로고
    • Conventional and saturation transfer EPR of spin labeled mutant bacteriophage M13 coat protein in phospholipid bilayers
    • Wolkers, W. F., Spruijt, R. B., Kaan, A., Konings, R. N. H., and Hemminga, M. A. (1997) Conventional and saturation transfer EPR of spin labeled mutant bacteriophage M13 coat protein in phospholipid bilayers, Biochim. Biophys. Acta 1327, 5-16.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 5-16
    • Wolkers, W.F.1    Spruijt, R.B.2    Kaan, A.3    Konings, R.N.H.4    Hemminga, M.A.5
  • 10
    • 0034694968 scopus 로고    scopus 로고
    • Localization and rearrangement modulation of the N-terminal arm of the membrane-bound major coat protein of bacteriophage M13
    • Spruijt, R. B., Meijer, A. B., Wolfs, C. J. A. M., and Hemminga, M. A. (2000) Localization and rearrangement modulation of the N-terminal arm of the membrane-bound major coat protein of bacteriophage M13, Biochim. Biophys. Acta 1509, 311-323.
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 311-323
    • Spruijt, R.B.1    Meijer, A.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 11
    • 0035979356 scopus 로고    scopus 로고
    • Membrane-anchoring interactions of M13 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M., and Hemminga, M. A. (2001) Membrane-anchoring interactions of M13 major coat protein, Biochemistry 40, 8815-8820.
    • (2001) Biochemistry , vol.40 , pp. 8815-8820
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 12
    • 0343185890 scopus 로고    scopus 로고
    • Structural and orientational information of the membrane embedded M13 coat protein by C-13-MAS NMR spectroscopy
    • Glaubitz, C., Grobner, G., and Watts, A. (2000) Structural and orientational information of the membrane embedded M13 coat protein by C-13-MAS NMR spectroscopy, Biochim. Biophys. Acta 1463, 151-161.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 151-161
    • Glaubitz, C.1    Grobner, G.2    Watts, A.3
  • 13
    • 0028058295 scopus 로고
    • Molecular models and structural comparisons of native and mutant class-I filamentous bacteriophages Ff (fd, f1, M13), If1 and Ike
    • Marvin, D. A., Hale, R. D., Nave, C., and Citterich, M. H. (1994) Molecular models and structural comparisons of native and mutant class-I filamentous bacteriophages Ff (fd, f1, M13), If1 and Ike, J. Mol. Biol. 235, 260-286.
    • (1994) J. Mol. Biol. , vol.235 , pp. 260-286
    • Marvin, D.A.1    Hale, R.D.2    Nave, C.3    Citterich, M.H.4
  • 14
    • 0026340802 scopus 로고
    • The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli
    • Spruijt, R. B., and Hemminga, M. A. (1991) The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli, Biochemistry 30, 11147-11154.
    • (1991) Biochemistry , vol.30 , pp. 11147-11154
    • Spruijt, R.B.1    Hemminga, M.A.2
  • 15
    • 0027414063 scopus 로고
    • Conformational states of mutant Ml3 coat proteins are regulated by transmembrane residues
    • Li, Z. M., Glibowicka, M., Joensson, C., and Deber, C. M. (1993) Conformational states of mutant Ml3 coat proteins are regulated by transmembrane residues, J. Biol. Chem. 268, 4584-4587.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4584-4587
    • Li, Z.M.1    Glibowicka, M.2    Joensson, C.3    Deber, C.M.4
  • 16
    • 0032577317 scopus 로고    scopus 로고
    • The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane
    • Haigh, N. G.. and Webster, R. E. (1998) The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane, J. Mol. Biol. 279, 19-29.
    • (1998) J. Mol. Biol. , vol.279 , pp. 19-29
    • Haigh, N.G.1    Webster, R.E.2
  • 17
    • 0141785142 scopus 로고    scopus 로고
    • Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition
    • Fernandes, F., Loura, L. M. S., Prieto, M., Koehorst, R. B. M., Spruijt, R. B., and Hemminga, M. A. (2003) Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition, Biophys. J. 85, 2430-2441.
    • (2003) Biophys. J. , vol.85 , pp. 2430-2441
    • Fernandes, F.1    Loura, L.M.S.2    Prieto, M.3    Koehorst, R.B.M.4    Spruijt, R.B.5    Hemminga, M.A.6
  • 18
    • 0037333304 scopus 로고    scopus 로고
    • Membrane proteins: The "Wild West" of structural biology
    • Torres, J., Stevens, T. J., and Samso, M. (2003) Membrane proteins: the "Wild West" of structural biology, Trends Biochem. Sci. 28, 137-144.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 137-144
    • Torres, J.1    Stevens, T.J.2    Samso, M.3
  • 19
    • 0029848950 scopus 로고    scopus 로고
    • Accessibility and environment probing using cysteine residues introduced along the putative transmembrane domain of the major coat protein of bacteriophage M13
    • Spruijt, R. B., Wolfs, C. J. A. M., Verver, J. W. G., and Hemminga, M. A. (1996) Accessibility and environment probing using cysteine residues introduced along the putative transmembrane domain of the major coat protein of bacteriophage M13, Biochemistry 35, 10383-10391.
    • (1996) Biochemistry , vol.35 , pp. 10383-10391
    • Spruijt, R.B.1    Wolfs, C.J.A.M.2    Verver, J.W.G.3    Hemminga, M.A.4
  • 20
    • 0029906010 scopus 로고    scopus 로고
    • Local dynamics of the M13 major coat protein in different membrane-mimicking systems
    • Stopar, D., Spruijt, R. B., Wolfs, C. J. A. M., and Hemminga, M. A. (1996) Local dynamics of the M13 major coat protein in different membrane-mimicking systems, Biochemistry 35, 15467-15473.
    • (1996) Biochemistry , vol.35 , pp. 15467-15473
    • Stopar, D.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 21
    • 0035942345 scopus 로고    scopus 로고
    • Configurations of the N-terminal amphipathic domain of the membrane-bound M13 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M., and Hemminga, M. A. (2001) Configurations of the N-terminal amphipathic domain of the membrane-bound M13 major coat protein, Biochemistry 40, 5081-5086.
    • (2001) Biochemistry , vol.40 , pp. 5081-5086
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 22
    • 0015820465 scopus 로고
    • Synthesis and Characterization of Two Fluorescent Sulfhydryl Reagents
    • Hudson, E. N., and Weber, G. (1973) Synthesis and Characterization of Two Fluorescent Sulfhydryl Reagents, Biochemistry 12, 4154-4161.
    • (1973) Biochemistry , vol.12 , pp. 4154-4161
    • Hudson, E.N.1    Weber, G.2
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 24
    • 0024468872 scopus 로고
    • Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13
    • Spruijt, R. B., Wolfs, C. J. A. M., and Hemminga, M. A. (1989) Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13, Biochemistry 28, 9158-9165.
    • (1989) Biochemistry , vol.28 , pp. 9158-9165
    • Spruijt, R.B.1    Wolfs, C.J.A.M.2    Hemminga, M.A.3
  • 25
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • De Planque, M. R. R., Goormagtigh, E., Greathouse, D. V., Koeppe, R. E., II, De Kruijtzer, J. A. W., Liskamp, R. M. J., De Kruijff, B., and Killian, J. A. (2001) Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation, Biochemistry 40, 5000-5010.
    • (2001) Biochemistry , vol.40 , pp. 5000-5010
    • De Planque, M.R.R.1    Goormagtigh, E.2    Greathouse, D.V.3    Koeppe II, R.E.4    De Kruijtzer, J.A.W.5    Liskamp, R.M.J.6    De Kruijff, B.7    Killian, J.A.8
  • 26
    • 0037117758 scopus 로고    scopus 로고
    • Importance of hydrophobic matching for spontaneous insertion of a single-spanning membrane protein
    • Ridder, A., van de Hoef, W., Stam, J., Kuhn, A., de Kruijff, B., and Killian, J. A. (2002) Importance of hydrophobic matching for spontaneous insertion of a single-spanning membrane protein, Biochemistry 41, 4946-4952.
    • (2002) Biochemistry , vol.41 , pp. 4946-4952
    • Ridder, A.1    Van De Hoef, W.2    Stam, J.3    Kuhn, A.4    De Kruijff, B.5    Killian, J.A.6
  • 27
    • 0017916757 scopus 로고
    • Solute quenching of protein fluorescence
    • Lehrer, S. S., and Leavis, P. C. (1978) Solute quenching of protein fluorescence, Methods Enzymol. 49, 222-236.
    • (1978) Methods Enzymol. , vol.49 , pp. 222-236
    • Lehrer, S.S.1    Leavis, P.C.2
  • 28
    • 0027370072 scopus 로고
    • Secondary structure of M13 coat protein in phospholipids studied by circular dichroism, Raman, and Fourier transform infrared spectroscopy
    • Sanders, J. C., Haris, P. I., Chapman, D., Otto, C., and Hemminga, M. A. (1993) Secondary structure of M13 coat protein in phospholipids studied by circular dichroism, Raman, and Fourier transform infrared spectroscopy, Biochemistry 32, 12446-12453.
    • (1993) Biochemistry , vol.32 , pp. 12446-12453
    • Sanders, J.C.1    Haris, P.I.2    Chapman, D.3    Otto, C.4    Hemminga, M.A.5
  • 29
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • Koehorst, R. B. M., Spruijt, R. B., Vergeldt, F. J., and Hemminga, M. A. (2004) Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy, Biophys. J. 87, 1445-1455.
    • (2004) Biophys. J. , vol.87 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4
  • 30
    • 0034705085 scopus 로고    scopus 로고
    • Membrane assembly of the bacteriophage Pf3 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M., and Hemminga, M. A. (2000) Membrane assembly of the bacteriophage Pf3 major coat protein, Biochemistry 39, 6157-6163.
    • (2000) Biochemistry , vol.39 , pp. 6157-6163
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 31
    • 0019230178 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. I. Cytoplasmic membrane and total phospholipids
    • Burnell, E., Van Alphen, L., Verkleij, A., and De Kruijff, B. (1980) Phosphorus-31 nuclear magnetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. I. Cytoplasmic membrane and total phospholipids, Biochim. Biophys. Acta 597, 492-501.
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 492-501
    • Burnell, E.1    Van Alphen, L.2    Verkleij, A.3    De Kruijff, B.4
  • 32
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. (1998) Hydrophobic mismatch between proteins and lipids in membranes, Biochim. Biophys. Acta 1376, 401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 33
    • 0026669051 scopus 로고
    • Spectroscopy of lipid protein interactions; Structural aspects of two different forms of the coat protein of bacteriophage M13 incorporated in model membranes
    • Hemminga, M. A., Sanders, J. C., and Spruijt, R. B. (1992) Spectroscopy of lipid protein interactions; Structural aspects of two different forms of the coat protein of bacteriophage M13 incorporated in model membranes, Prog. Lipid Res. 31, 301-333.
    • (1992) Prog. Lipid Res. , vol.31 , pp. 301-333
    • Hemminga, M.A.1    Sanders, J.C.2    Spruijt, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.