2IZW

Crystal structure of Ryegrass Mottle Virus

2IZW の概要

• エントリーDOI: 10.2210/pdb2izw/pdb
• 分子名称: RYEGRASS MOTTLE VIRUS COAT PROTEIN (1 entity in total)
• 機能のキーワード: rna, virus, assembly, capsid protein
• 由来する生物種: RYEGRASS MOTTLE VIRUS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76571.65

構造登録者

Plevka, P.,Tars, K.,Zeltins, A.,Balke, I.,Truve, E.,Liljas, L. (登録日: 2006-07-27, 公開日: 2007-10-02, 最終更新日: 2023-12-13)

主引用文献

Plevka, P.,Tars, K.,Zeltins, A.,Balke, I.,Truve, E.,Liljas, L.
The Three-Dimensional Structure of Ryegrass Mottle Virus at 2.9 A Resolution.
Virology, 369:364-, 2007

PubMed Abstract: The crystal structure of the sobemovirus Ryegrass mottle virus (RGMoV) has been determined at 2.9 A resolution. The coat protein has a canonical jellyroll beta-sandwich fold. In comparison to other sobemoviruses the RGMoV coat protein is missing several residues in two of the loop regions. The first loop contributes to contacts between subunits around the quasi-threefold symmetry axis. The altered contact interface results in tilting of the subunits towards the quasi-threefold axis. The assembly of the T=3 capsid of sobemoviruses is controlled by the N-termini of C subunits forming a so-called beta-annulus. The other loop that is smaller in the RGMoV structure contains a helix that participates in stabilization of the beta-annulus in other sobemoviruses. The loss of interaction between the RGMoV loop and the beta-annulus has been compensated for by additional interactions between the N-terminal arms. As a consequence of these differences, the diameter of the RGMoV particle is 8 A smaller than that of the other sobemoviruses. The interactions of coat proteins in sobemovirus capsids involve calcium ions. Depletion of calcium ions results in particle swelling, which is considered a first step in disassembly. We could not identify any density for metal ions in the proximity of the conserved residues normally involved in calcium binding, but the RGMoV structure does not show any signs of swelling. A likely reason is the low pH (3.0) of the crystallization buffer in which the groups interacting with the calcium ions are not charged.

PubMed: 17881031
DOI: 10.1016/J.VIROL.2007.07.028

実験手法

X-RAY DIFFRACTION (2.9 Å)