6G41

Crystal structure of SeMet-labeled mavirus penton protein

6G41 の概要

• エントリーDOI: 10.2210/pdb6g41/pdb
• 分子名称: Minor capsid protein (1 entity in total)
• 機能のキーワード: single jelly-roll, capsid protein, virus, viral protein
• 由来する生物種: Cafeteriavirus-dependent mavirus
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 358559.84

構造登録者

Born, D.,Reuter, L.,Meinhart, A.,Reinstein, J. (登録日: 2018-03-26, 公開日: 2018-07-04, 最終更新日: 2024-11-20)

主引用文献

Born, D.,Reuter, L.,Mersdorf, U.,Mueller, M.,Fischer, M.G.,Meinhart, A.,Reinstein, J.
Capsid protein structure, self-assembly, and processing reveal morphogenesis of the marine virophage mavirus.
Proc. Natl. Acad. Sci. U.S.A., 115:7332-7337, 2018

PubMed Abstract: Virophages have the unique property of parasitizing giant viruses within unicellular hosts. Little is understood about how they form infectious virions in this tripartite interplay. We provide mechanistic insights into assembly and maturation of mavirus, a marine virophage, by combining structural and stability studies on capsomers, virus-like particles (VLPs), and native virions. We found that the mavirus protease processes the double jelly-roll (DJR) major capsid protein (MCP) at multiple C-terminal sites and that these sites are conserved among virophages. Mavirus MCP assembled in in the absence and presence of penton protein, forming VLPs with defined size and shape. While quantifying VLPs in lysates, we found that full-length rather than processed MCP is the competent state for capsid assembly. Full-length MCP was thermally more labile than truncated MCP, and crystal structures of both states indicate that full-length MCP has an expanded DJR core. Thus, we propose that the MCP C-terminal domain serves as a scaffolding domain by adding strain on MCP to confer assembly competence. Mavirus protease processed MCP more efficiently after capsid assembly, which provides a regulation mechanism for timing capsid maturation. By analogy to Sputnik and adenovirus, we propose that MCP processing renders mavirus particles infection competent by loosening interactions between genome and capsid shell and destabilizing pentons for genome release into host cells. The high structural similarity of mavirus and Sputnik capsid proteins together with conservation of protease and MCP processing suggest that assembly and maturation mechanisms described here are universal for virophages.

PubMed: 29941605
DOI: 10.1073/pnas.1805376115

実験手法

X-RAY DIFFRACTION (2.9 Å)