9JPR

Local refinement of H11 nanotubes assembled from baculovirus capsid protein

9JPR の概要

• エントリーDOI: 10.2210/pdb9jpr/pdb
• EMDBエントリー: 61712
• 分子名称: Glutathione S-transferase class-mu 26 kDa isozyme,Viral capsid 39 protein (1 entity in total)
• 機能のキーワード: capsid protein, self-assembly, baculovirus, nanotube, viral protein
• 由来する生物種: Schistosoma japonicum (Blood fluke); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 484201.41

構造登録者

Tian, K.,Rao, G.,Fu, Y.,Cao, S. (登録日: 2024-09-26, 公開日: 2025-10-22, 最終更新日: 2026-01-28)

主引用文献

Tian, K.,Na, H.,Fu, Y.,Chong, T.,Leng, C.,Meng, F.,Liang, Y.,Wang, M.,Hu, Z.,Wang, X.,Rao, G.,Cao, S.
Structural polymorphism of two-dimensional lattices assembled from baculoviral capsid proteins.
Virol Sin, 40:935-945, 2025

PubMed Abstract: Protein nanotubes (PNTs) can be regarded as two-dimensional (2D) lattices with p1 or p2 symmetry rolled into tubes. However, attempts to re-assemble their building blocks into stable 2D nanomaterials often fail. Here, starting from two baculoviral capsid proteins, we screened protein variants for the in vitro assembly of various nanotubes and nanosheets. These high-order assemblies were structurally characterized by cryo-electron microscopy techniques. Interfacial analysis of three groups of PNTs revealed that helical heterogeneity is largely the result of the redundancy of p2 symmetry-related contacting interfaces. The assembled nanosheets showed similar interfacial networks to their nanotubular counterparts. In addition, foreign macromolecules could be efficiently displayed on the size-controllable double-layered nanosheets. This study sheds light on the rational design of flexible nanosheets, and it also provides novel 2D protein scaffolds for developing biocompatible materials.

PubMed: 41265796
DOI: 10.1016/j.virs.2025.11.005

実験手法

ELECTRON MICROSCOPY (2.8 Å)