1NH4

Structure of the coat protein in fd filamentous bacteriophage particles

1NH4 の概要

• エントリーDOI: 10.2210/pdb1nh4/pdb
• 関連するPDBエントリー: 1IFI
• NMR情報: BMRB: 5815
• 分子名称: Major coat protein (1 entity in total)
• 機能のキーワード: alpha helix, helical virus, virus
• 由来する生物種: Enterobacteria phage fd
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5212.02

構造登録者

Zeri, A.C.,Mesleh, M.F.,Nevzorov, A.A.,Opella, S.J. (登録日: 2002-12-18, 公開日: 2003-05-06, 最終更新日: 2024-05-22)

主引用文献

Zeri, A.C.,Mesleh, M.F.,Nevzorov, A.A.,Opella, S.J.
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
Proc.Natl.Acad.Sci.USA, 100:6458-6463, 2003

PubMed 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.

PubMed: 12750469
DOI: 10.1073/pnas.1132059100

実験手法

SOLID-STATE NMR