1PJF

Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage

1PJF の概要

• エントリーDOI: 10.2210/pdb1pjf/pdb
• NMR情報: BMRB: 5877
• 分子名称: COAT PROTEIN B (1 entity in total)
• 機能のキーワード: viral protein, helical virus
• 由来する生物種: Pseudomonas phage Pf1
• 細胞内の位置: Virion (Potential): P03621
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4612.39

構造登録者

Thiriot, D.S.,Nevzorov, A.A.,Zagyanskiy, L.,Wu, C.H.,Opella, S.J. (登録日: 2003-06-02, 公開日: 2004-08-10, 最終更新日: 2024-05-01)

主引用文献

Thiriot, D.S.,Nevzorov, A.A.,Zagyanskiy, L.,Wu, C.H.,Opella, S.J.
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
J.Mol.Biol., 341:869-879, 2004

PubMed Abstract: 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 neutron diffraction, the structure of its membrane-bound form, and the structure of fd coat protein. These structural comparisons provide insights into several biological properties, differences between class I and class II filamentous bacteriophages, and the assembly process. The six N-terminal amino acid residues adopt an unusual "double hook" conformation on the outside of the bacteriophage particle. The solid-state NMR results indicate that at 30 degrees C, some of the coat protein subunits assume a single, fully structured conformation, and some have a few mobile residues that provide a break between two helical segments, in agreement with structural models from X-ray fiber and neutron diffraction, respectively. The atomic resolution structure determined by solid-state NMR for residues 7-14 and 18-46, which excludes the N-terminal double hook and the break between the helical segments, but encompasses more than 80% of the backbone including the distinct kink at residue 29, agrees with that determined by X-ray fiber diffraction with an RMSD value of 2.0 A. The symmetry and distance constraints determined by X-ray fiber and neutron diffraction enable the construction of an accurate model of the bacteriophage particle from the coordinates of the coat protein monomers.

PubMed: 15288792
DOI: 10.1016/j.jmb.2004.06.038

実験手法

SOLID-STATE NMR