1ZN5

Solid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage

Summary for 1ZN5

• Entry DOI: 10.2210/pdb1zn5/pdb
• Related: 1PJF
• NMR Information: BMRB: 5877
• Descriptor: Coat protein B (1 entity in total)
• Functional Keywords: alpha-helix, virion, orientational constraints, helical virus, 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.,Opella, S.J. (deposition date: 2005-05-11, release date: 2005-05-17, Last modification date: 2024-05-22)

Primary citation

Thiriot, D.S.,Nevzorov, A.A.,Opella, S.J.
Structural basis of the temperature transition of Pf1 bacteriophage.
Protein Sci., 14:1064-1070, 2005

PubMed Abstract: 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.

PubMed: 15741342
DOI: 10.1110/ps.041220305

Experimental method

SOLID-STATE NMR