Work

Structural basis of the temperature transition of Pf1 bacteriophage

Year: 2005

Type: article

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.

Source: Protein Science

DOI: 10.1110/ps.041220305

Authors: David S. Thiriot, Alexander A. Nevzorov, Stanley J. Opella

Institution: University of California San Diego

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Biomedical Imaging and Bioengineering

Awards: NMR Studies of Biological Supramolecular Structures, Resource for NMR Molecular Imaging of Proteins, Discovery and NMR Structure of HIV1 Vpu-binding Peptides, SOLID STATE NMR OF PEPTIDES