1pjf
From Proteopedia
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Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage
Overview
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.
About this Structure
1PJF is a Single protein structure of sequence from Pseudomonas phage pf1. Full crystallographic information is available from OCA.
Reference
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy., Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ, J Mol Biol. 2004 Aug 13;341(3):869-79. PMID:15288792
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