3IYS

Homology model of avian polyomavirus asymmetric unit

3IYS の概要

• エントリーDOI: 10.2210/pdb3iys/pdb
• 関連するPDBエントリー: 1SIE
• EMDBエントリー: 5180
• 分子名称: Major capsid protein VP1 (1 entity in total)
• 機能のキーワード: avian, polyomavirus, apv, icosahedral virus, virus
• 由来する生物種: Budgerigar fledgling disease polyomavirus (BFPyV)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 224696.60

構造登録者

Shen, P.S.,Enderlein, D.,Nelson, C.D.S.,Carter, W.S.,Kawano, M.,Xing, L.,Swenson, R.D.,Olson, N.H.,Baker, T.S.,Cheng, R.H.,Atwood, W.J.,Johne, R.,Belnap, D.M. (登録日: 2010-04-19, 公開日: 2011-01-26, 最終更新日: 2024-02-21)

主引用文献

Shen, P.S.,Enderlein, D.,Nelson, C.D.,Carter, W.S.,Kawano, M.,Xing, L.,Swenson, R.D.,Olson, N.H.,Baker, T.S.,Cheng, R.H.,Atwood, W.J.,Johne, R.,Belnap, D.M.
The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4.
Virology, 411:142-152, 2011

PubMed Abstract: Avian polyomavirus (APV) causes a fatal, multi-organ disease among several bird species. Using cryogenic electron microscopy and other biochemical techniques, we investigated the structure of APV and compared it to that of mammalian polyomaviruses, particularly JC polyomavirus and simian virus 40. The structure of the pentameric major capsid protein (VP1) is mostly conserved; however, APV VP1 has a unique, truncated C-terminus that eliminates an intercapsomere-connecting β-hairpin observed in other polyomaviruses. We postulate that the terminal β-hairpin locks other polyomavirus capsids in a stable conformation and that absence of the hairpin leads to the observed capsid size variation in APV. Plug-like density features were observed at the base of the VP1 pentamers, consistent with the known location of minor capsid proteins VP2 and VP3. However, the plug density is more prominent in APV and may include VP4, a minor capsid protein unique to bird polyomaviruses.

PubMed: 21239031
DOI: 10.1016/j.virol.2010.12.005

実験手法

ELECTRON MICROSCOPY (11.3 Å)