8I8A

Cryo-EM structure of the major capsid protein VP39 of Autographa californica multiple nucleopolyhedrovirus (AcMNPV)

8I8A の概要

• エントリーDOI: 10.2210/pdb8i8a/pdb
• EMDBエントリー: 35242 35245
• 分子名称: Major viral capsid protein (1 entity in total)
• 機能のキーワード: virus, capsid protein, viral protein
• 由来する生物種: Autographa californica multiple nucleopolyhedrovirus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77982.22

構造登録者

Jia, X.,Zhang, Q. (登録日: 2023-02-03, 公開日: 2023-12-13, 最終更新日: 2024-10-16)

主引用文献

Jia, X.,Gao, Y.,Huang, Y.,Sun, L.,Li, S.,Li, H.,Zhang, X.,Li, Y.,He, J.,Wu, W.,Venkannagari, H.,Yang, K.,Baker, M.L.,Zhang, Q.
Architecture of the baculovirus nucleocapsid revealed by cryo-EM.
Nat Commun, 14:7481-7481, 2023

PubMed Abstract: Baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV) has been widely used as a bioinsecticide and a protein expression vector. Despite their importance, very little is known about the structure of most baculovirus proteins. Here, we show a 3.2 Å resolution structure of helical cylindrical body of the AcMNPV nucleocapsid, composed of VP39, as well as 4.3 Å resolution structures of both the head and the base of the nucleocapsid composed of over 100 protein subunits. AcMNPV VP39 demonstrates some features of the HK97-like fold and utilizes disulfide-bonds and a set of interactions at its C-termini to mediate nucleocapsid assembly and stability. At both ends of the nucleocapsid, the VP39 cylinder is constricted by an outer shell ring composed of proteins AC104, AC142 and AC109. AC101(BV/ODV-C42) and AC144(ODV-EC27) form a C14 symmetric inner layer at both capsid head and base. In the base, these proteins interact with a 7-fold symmetric capsid plug, while a portal-like structure is seen in the central portion of head. Additionally, we propose an application of AlphaFold2 for model building in intermediate resolution density.

PubMed: 37980340
DOI: 10.1038/s41467-023-43284-1

実験手法

ELECTRON MICROSCOPY (3.21 Å)