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 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.

PMID: 15288792 [PubMed - indexed for MEDLINE]



Source: PubMed