1zn5
From Proteopedia
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Solid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage
Overview
The filamentous bacteriophage Pf1 undergoes a reversible, temperature-dependent transition that is also influenced by salt, concentrations. This structural responsiveness may be a manifestation of, the important biological property of flexibility, which is necessary for, long, thin filamentous assemblies as a protection against shear forces. To, investigate structural changes in the major coat protein, one- and, two-dimensional solid-state NMR spectra of concentrated solutions of Pf1, bacteriophage were acquired, and the structure of the coat protein, determined at 0 degrees C was compared with the structure previously, determined at 30 degrees C. Despite dramatic differences in the NMR, spectra, the overall change in the coat protein structure is small., Changes in the orientation of the C-terminal helical segment and the, conformation of the first five residues at the N-terminus are apparent., These results are consistent with prior studies by X-ray fiber diffraction, and other biophysical methods.
About this Structure
1ZN5 is a Single protein structure of sequence from Pseudomonas phage pf1. Full crystallographic information is available from OCA.
Reference
Structural basis of the temperature transition of Pf1 bacteriophage., Thiriot DS, Nevzorov AA, Opella SJ, Protein Sci. 2005 Apr;14(4):1064-70. Epub 2005 Mar 1. PMID:15741342
Page seeded by OCA on Wed Nov 21 07:32:53 2007
