4BP7

Asymmetric structure of a virus-receptor complex

これはPDB形式変換不可エントリーです。

4BP7 の概要

• エントリーDOI: 10.2210/pdb4bp7/pdb
• EMDBエントリー: 2365
• 分子名称: COAT PROTEIN (1 entity in total)
• 機能のキーワード: virus, bacteriophage
• 由来する生物種: ENTEROBACTERIA PHAGE MS2
• 細胞内の位置: Virion : P03612
• タンパク質・核酸の鎖数: 180
• 化学式量合計: 2472923.52

構造登録者

Dent, K.C.,Thompson, R.,Barker, A.M.,Barr, J.N.,Hiscox, J.A.,Stockley, P.G.,Ranson, N.A. (登録日: 2013-05-23, 公開日: 2013-07-17, 最終更新日: 2024-05-08)

主引用文献

Dent, K.C.,Thompson, R.,Barker, A.M.,Hiscox, J.A.,Barr, J.N.,Stockley, P.G.,Ranson, N.A.
The Asymmetric Structure of an Icosahedral Virus Bound its Receptor Suggests a Mechanism for Genome Release.
Structure, 21:1225-1234, 2013

PubMed Abstract: Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus. Cryo-electron tomography and subtomographic averaging of such complexes result in a structure containing clear density for the packaged genome, implying that the conformation of the genome is the same in each virus particle. The data also suggest that the single-copy viral maturation protein breaks the symmetry of the capsid, occupying a position that would be filled by a coat protein dimer in an icosahedral shell. This capsomere can thus fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection.

PubMed: 23810697
DOI: 10.1016/J.STR.2013.05.012

実験手法

ELECTRON MICROSCOPY (39 Å)