1PJF
Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage
Summary for 1PJF
Entry DOI | 10.2210/pdb1pjf/pdb |
NMR Information | BMRB: 5877 |
Descriptor | COAT PROTEIN B (1 entity in total) |
Functional Keywords | viral protein, helical virus |
Biological source | Pseudomonas phage Pf1 |
Cellular location | Virion (Potential): P03621 |
Total number of polymer chains | 1 |
Total formula weight | 4612.39 |
Authors | Thiriot, D.S.,Nevzorov, A.A.,Zagyanskiy, L.,Wu, C.H.,Opella, S.J. (deposition date: 2003-06-02, release date: 2004-08-10, Last modification date: 2024-05-01) |
Primary citation | 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 Cited by 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: 15288792DOI: 10.1016/j.jmb.2004.06.038 PDB entries with the same primary citation |
Experimental method | SOLID-STATE NMR |
Structure validation
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