1ZN5

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

1ZN5 の概要

• エントリーDOI: 10.2210/pdb1zn5/pdb
• 関連するPDBエントリー: 1PJF
• NMR情報: BMRB: 5877
• 分子名称: Coat protein B (1 entity in total)
• 機能のキーワード: alpha-helix, virion, orientational constraints, helical virus, virus
• 由来する生物種: Pseudomonas phage Pf1
• 細胞内の位置: Virion (Potential): P03621
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4612.39

構造登録者

Thiriot, D.S.,Nevzorov, A.A.,Opella, S.J. (登録日: 2005-05-11, 公開日: 2005-05-17, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLID-STATE NMR