2VQ0

Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)

2VQ0 の概要

• エントリーDOI: 10.2210/pdb2vq0/pdb
• 関連するPDBエントリー: 1SMV 1VAK 1VB2 1VB4 1X33 1X35 1X36
• 分子名称: COAT PROTEIN, CALCIUM ION (2 entities in total)
• 機能のキーワード: capsid protein, sesbania mosaic virus, virion, beta-annulus, coat protein, virus assembly, viral protein
• 由来する生物種: SESBANIA MOSAIC VIRUS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 82867.38

構造登録者

Anju, P.,Subashchandrabose, C.,Satheshkumar, P.S.,Savithri, H.S.,Murthy, M.R.N. (登録日: 2008-03-10, 公開日: 2008-05-13, 最終更新日: 2024-11-06)

主引用文献

Anju, P.,Subashchandrabose, C.,Satheshkumar, P.S.,Savithri, H.S.,Murthy, M.R.N.
Structure of Recombinant Capsids Formed by the Beta-Annulus Deletion Mutant-Rcp (Delta 48-59) of Sesbania Mosaic Virus
Virology, 375:190-, 2008

PubMed Abstract: A unique feature of several T=3 icosahedral viruses is the presence of a structure called the beta-annulus formed by extensive hydrogen bonding between protein subunits related by icosahedral three-fold axis of symmetry. This unique structure has been suggested as a molecular switch that determines the T=3 capsid assembly. In order to examine the importance of the beta-annulus, a deletion mutant of Sesbania mosaic virus coat protein in which residues 48-59 involved in the formation of the beta-annulus were deleted retaining the rest of the residues in the amino terminal segment (rCP (Delta48-59)) was constructed. When expressed in Escherichia coli, the mutant protein assembled into virus like particles of sizes close to that of the wild type virus particles. The purified capsids were crystallized and their three dimensional structure was determined at 3.6 A resolution by X-ray crystallography. The mutant capsid structure closely resembled that of the native virus particles. However, surprisingly, the structure revealed that the assembly of the particles has proceeded without the formation of the beta-annulus. Therefore, the beta-annulus is not essential for T=3 capsid assembly as speculated earlier and may be formed as a consequence of the particle assembly. This is the first structural demonstration that the virus particle morphology with and without the beta-annulus could be closely similar.

PubMed: 18295296
DOI: 10.1016/J.VIROL.2008.01.023

実験手法

X-RAY DIFFRACTION (3.6 Å)