5G5O

Structure of the snake adenovirus 1 hexon-interlacing LH3 protein, native

5G5O の概要

• エントリーDOI: 10.2210/pdb5g5o/pdb
• 関連するPDBエントリー: 5G5N
• 分子名称: LH3 HEXON-INTERLACING CAPSID PROTEIN, ACETATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: viral protein, capsid protein, beta-helix
• 由来する生物種: SNAKE ADENOVIRUS 1
• 細胞内の位置: Virion : A9CB85
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 243046.55

構造登録者

Nguyen, T.H.,Singh, A.K.,Albala-Perez, B.,van Raaij, M.J. (登録日: 2016-05-26, 公開日: 2017-06-07, 最終更新日: 2024-01-10)

主引用文献

Menendez-Conejero, R.,Nguyen, T.H.,Singh, A.K.,Condezo, G.N.,Marschang, R.E.,van Raaij, M.J.,San Martin, C.
Structure of a Reptilian Adenovirus Reveals a Phage Tailspike Fold Stabilizing a Vertebrate Virus Capsid.
Structure, 25:1562-1573, 2017

PubMed Abstract: Although non-human adenoviruses (AdVs) might offer solutions to problems posed by human AdVs as therapeutic vectors, little is known about their basic biology. In particular, there are no structural studies on the complete virion of any AdV with a non-mammalian host. We combine mass spectrometry, cryo-electron microscopy, and protein crystallography to characterize the composition and structure of a snake AdV (SnAdV-1, Atadenovirus genus). SnAdV-1 particles contain the genus-specific proteins LH3, p32k, and LH2, a previously unrecognized structural component. Remarkably, the cementing protein LH3 has a trimeric β helix fold typical of bacteriophage host attachment proteins. The organization of minor coat proteins differs from that in human AdVs, correlating with higher thermostability in SnAdV-1. These findings add a new piece to the intriguing puzzle of virus evolution, hint at the use of cell entry pathways different from those in human AdVs, and will help development of new, thermostable SnAdV-1-based vectors.

PubMed: 28943338
DOI: 10.1016/j.str.2017.08.007

実験手法

X-RAY DIFFRACTION (2 Å)