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Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.

ABSTRACT: 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.

SUBMITTER: Zeri AC

PROVIDER: S-EPMC164468 | biostudies-literature | 2003 May

REPOSITORIES: biostudies-literature

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Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.

Zeri Ana Carolina AC Mesleh Michael F MF Nevzorov Alexander A AA Opella Stanley J SJ

Proceedings of the National Academy of Sciences of the United States of America 20030515 11

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 sh ...[more]

PMID: 12750469

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Dataset Information

Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.

Publications

Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.

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