Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.

The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS micelles, stearate was added, spin-labeled at the 5- or 16-position with a doxyl group containing a stable nitroxide radical. The average position of the spin-labels in the micelles was derived from the line broadening of the resonances in the 13C spectrum of SDS. Subsequently, we derived a model of the relative position of gVIIIp in the SDS micelle from the effect of the spin-labels on the gVIIIp resonances, monitored via 1H-15N HSQC and TOCSY experiments. The results are consistent with the structure of gVIIIp having two helical strands. One strand is a long hydrophobic helix that spans the micelle, and the other is a shorter amphipathic helix on the surface of the micelle. These results are in good agreement with the structure of gVIIIp in membranes proposed by McDonnell et al. on the basis of solid state NMR data [McDonnell, P. A., Shon, K., Kim, Y., & Opella, S. J. (1993) J. Mol. Biol. 233, 447-463]. This study indicates that high-resolution NMR on this membrane protein, solubilized in detergent micelles, is a very suitable technique for mimicking these proteins in their natural environment. Furthermore, the data indicate that the structure of the micelle near the C-terminus of the major coat protein is distorted.(ABSTRACT TRUNCATED AT 250 WORDS)

[1]  S. Opella,et al.  fd coat protein structure in membrane environments. , 1993, Journal of molecular biology.

[2]  M. L. Remerowski,et al.  Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. , 1993, Biochemistry.

[3]  L. Makowski,et al.  Terminating a macromolecular helix. Structural model for the minor proteins of bacteriophage M13. , 1992, Journal of molecular biology.

[4]  L. Makowski,et al.  Three-dimensional structure of a cloning vector. X-ray diffraction studies of filamentous bacteriophage M13 at 7 A resolution. , 1992, Journal of molecular biology.

[5]  B. Sykes,et al.  Assignment of amide 1H and 15N NMR resonances in detergent-solubilized M13 coat protein: a model for the coat protein dimer. , 1992, Biochemistry.

[6]  R. Spruijt,et al.  Spectroscopy of lipid-protein interactions: structural aspects of two different forms of the coat protein of bacteriophage M13 incorporated in model membranes. , 1992, Progress in lipid research.

[7]  R. Spruijt,et al.  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. , 1991, Biochemistry.

[8]  T. Poile,et al.  A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane. , 1991, Biochimica et biophysica acta.

[9]  L. Kay,et al.  Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix. , 1991, Biochemistry.

[10]  S. Opella,et al.  NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. , 1991, Science.

[11]  B. Sykes,et al.  Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein. , 1990, Biochemistry.

[12]  G. Wider,et al.  Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutions , 1989 .

[13]  R. Spruijt,et al.  Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13. , 1989, Biochemistry.

[14]  B. Sykes,et al.  Structure and dynamics of a detergent-solubilized membrane protein: measurement of amide hydrogen exchange rates in M13 coat protein by 1H NMR spectroscopy. , 1988, Biochemistry.

[15]  W. Wickner.  Mechanisms of membrane assembly: general lessons from the study of M13 coat protein and Escherichia coli leader peptidase. , 1988, Biochemistry.

[16]  L. Makowski,et al.  Conformation of the coat protein of filamentous bacteriophage Pf1 determined by neutron diffraction from magnetically oriented gels of specifically deuterated virions. , 1988, Journal of molecular biology.

[17]  A. Visser,et al.  Time-resolved tryptophan fluorescence anisotropy investigation of bacteriophage M13 coat protein in micelles and mixed bilayers. , 1987, Biochemistry.

[18]  B. Sykes,et al.  Backbone dynamics of a model membrane protein: assignment of the carbonyl carbon 13C NMR resonances in detergent-solubilized M13 coat protein. , 1987, Biochemistry.

[19]  B. Sykes,et al.  Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein. , 1986, Biochemistry.

[20]  S. Opella,et al.  Protein structure by solid state nuclear magnetic resonance. Residues 40 to 45 of bacteriophage fd coat protein. , 1985, Journal of molecular biology.

[21]  L. Kevan,et al.  Electron spin-echo modulation studies of doxylstearic acid spin probes in sodium and tetramethylammonium dodecyl sulfate micelles: interaction of the spin probe with deuterated water and with deuterated terminal methyl groups in the surfactant molecules , 1985 .

[22]  Ken A. Dill,et al.  Molecular conformations in surfactant micelles , 1984, Nature.

[23]  K. Wüthrich,et al.  Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. , 1983, Biochemical and biophysical research communications.

[24]  Pierre Plateau,et al.  Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequences , 1982 .

[25]  L. Kevan,et al.  Spatial-dependent electron scavenging by stearic acid nitroxide spin-labels in the photoionization of N,N,N',N'-tetramethylbenzidine in sodium dodecyl sulfate micelles , 1982 .

[26]  W. Wickner,et al.  The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediates. , 1982, The Journal of biological chemistry.

[27]  K. Dill.  Configurations of the amphiphilic molecules in micelles , 1982 .

[28]  K. Wüthrich,et al.  High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface. , 1982, Biophysical journal.

[29]  K. Wüthrich,et al.  Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies. , 1981, Biochimica et biophysica acta.

[30]  D. Banner,et al.  Structure of the protein and DNA in fd filamentous bacterial virus , 1981, Nature.

[31]  J. Gelan,et al.  Occurrence of chain folding in micelles: A 13C NMR relaxation and photophysical study , 1980 .

[32]  S. Opella,et al.  Structural properties of fd coat protein in sodium dodecyl sulfate micelles. , 1980, Biochemical and biophysical research communications.

[33]  G. Bodenhausen,et al.  Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy , 1980 .

[34]  R. Konings.  Template function of restriction enzyme fragments of phage M13 replicative form DNA. , 1980, Methods in enzymology.

[35]  F. Menger,et al.  On the structure of micelles , 1979 .

[36]  C. Tanford,et al.  Conformational states of a hydrophobic protein. The coat protein of fd bacteriophage. , 1978, Biochemistry.

[37]  U. Kragh-Hansen,et al.  Complexes of aliphatic sulfates and human-serum albumin studied by 13C nuclear-magnetic-resonance spectroscopy. , 1976, European journal of biochemistry.

[38]  W. Wickner.  Asymmetric orientation of a phage coat protein in cytoplasmic membrane of Escherichia coli. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[39]  C. Polnaszek,et al.  The fluidity and organization of mitochondrial membrane lipids of the brown adipose tissue of cold-adapted rats and hamsters as determined by nitroxide spin probes. , 1975, Archives of biochemistry and biophysics.

[40]  W. Hubbell,et al.  Molecular motion in spin-labeled phospholipids and membranes. , 1971, Journal of the American Chemical Society.

[41]  P. Hofschneider,et al.  Gene Order of RNA Bacteriophage M12 , 1970, Nature.

[42]  H. Hoffmann-Berling,et al.  A coat protein from bacteriophage fd. II. Interaction of the protein with DNA in vitro. , 1966, Journal of molecular biology.