%0 Journal Article %1 thiriot_structure_2004 %A Thiriot, David S %A Nevzorov, Alexander A %A Zagyanskiy, Lena %A Wu, Chin H %A Opella, Stanley J %D 2004 %J J. Mol. Biol. %K Bacteriophage Conformation,Protein Diffraction,X-Rays Pf1,Bacteriophages,Capsid Proteins,Magnetic Resonance Spectroscopy,Neutrons,Protein Structure,Software,Statistics Topic,Temperature,Tertiary,X-Ray as %N 3 %P 869--879 %R 10.1016/j.jmb.2004.06.038 %T Structure of the coat protein in \Pf\1 bacteriophage determined by solid-state \NMR\ spectroscopy %V 341 %X 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.

@article{thiriot_structure_2004, 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Thiriot, David S and Nevzorov, Alexander A and Zagyanskiy, Lena and Wu, Chin H and Opella, Stanley J}, biburl = {https://www.bibsonomy.org/bibtex/229556fafe91f158c5d337482a444c1a2/nmrresource}, doi = {10.1016/j.jmb.2004.06.038}, interhash = {41cfc4bbd4a0f2c19d317b3e0fc8b4d9}, intrahash = {29556fafe91f158c5d337482a444c1a2}, issn = {0022-2836}, journal = {J. Mol. Biol.}, keywords = {Bacteriophage Conformation,Protein Diffraction,X-Rays Pf1,Bacteriophages,Capsid Proteins,Magnetic Resonance Spectroscopy,Neutrons,Protein Structure,Software,Statistics Topic,Temperature,Tertiary,X-Ray as}, month = aug, number = 3, pages = {869--879}, pmid = {15288792}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Structure of the coat protein in {\{}Pf{\}}1 bacteriophage determined by solid-state {\{}NMR{\}} spectroscopy}}, volume = 341, year = 2004 }