The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1-5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly 15N-labeled 50-residue protein in a 1.6 x 107 Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of approximately 1A.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Eur Biophys J. 2011 Mar;40(3):221-34
Authors: Straus SK, Scott WR, Schwieters CD, Marvin DA
Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as...
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[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
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[NMR paper] Structure of a malaria parasite antigenic determinant displayed on filamentous bacter
Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: implications for the structure of continuous peptide epitopes of proteins.
Related Articles Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: implications for the structure of continuous peptide epitopes of proteins.
Protein Sci. 2001 Jun;10(6):1150-9
Authors: Monette M, Opella SJ, Greenwood J, Willis AE, Perham RN
The NANP repeating sequence of...
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11-19-2010 08:32 PM
[NMR paper] Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by sol
Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
Biochemistry. 1996 Apr 23;35(16):5145-57
Authors: Williams KA, Farrow NA, Deber CM, Kay LE
The structure and dynamics of the 53-residue filamentous bacteriophage IKe major coat protein in fully protonated myristoyllysophosphatidylglycerol (MPG)...
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08-22-2010 02:27 PM
[NMR paper] NMR studies of the major coat protein of bacteriophage M13. Structural information of
NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.
Eur J Biochem. 1995 Sep 1;232(2):490-500
Authors: Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ
The membrane-bound...
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[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Biochemistry. 1994 Nov 8;33(44):12990-7
Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ
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...
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[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
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[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Related Articles NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....