1pjf
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjf OCA], [http://www.ebi.ac.uk/pdbsum/1pjf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pjf RCSB]</span> | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:28 2008'' |
Revision as of 20:00, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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