9VEL
The composite cryo-EM structure of bacteriophage SPO1 capsid
9VEL の概要
| エントリーDOI | 10.2210/pdb9vel/pdb |
| EMDBエントリー | 65011 |
| 分子名称 | Gp6.1, Gp29.2, Gp2.7, ... (4 entities in total) |
| 機能のキーワード | spo1, phage, capsid, virus |
| 由来する生物種 | Bacillus phage SPO1 詳細 |
| タンパク質・核酸の鎖数 | 22 |
| 化学式量合計 | 919665.62 |
| 構造登録者 | |
| 主引用文献 | Zhao, X.,Wang, A.,Wang, Y.,Kang, Y.,Shao, Q.,Li, L.,Zheng, Y.,Hu, H.,Li, X.,Fan, H.,Cai, C.,Liu, B.,Fang, Q. Capsid structure of phage SPO1 reveals novel minor capsid proteins and insights into capsid stabilization. Structure, 33:1844-, 2025 Cited by PubMed Abstract: SPO1-related bacteriophages are promising candidates for phage therapy. We present the 3.0 Å cryo-electron microscopy (cryo-EM) structure of the SPO1 capsid with a triangulation number T = 16, enabling the construction of an atomic model comprising the major capsid protein and three types of minor capsid proteins: gp29.2, gp2.7, and gp36.3. These minor capsid proteins adopt novel folds. They might stabilize the capsid and determine its curvature. Gp29.2 monomers contain a three-blade propeller fold and are located at the 3-fold and quasi-three-fold axes. Gp2.7 forms pentamers atop pentameric capsomers, while gp36.3 binds to the capsid's inner surface, forming star-shaped structures increasing connections between pentameric and hexameric capsomers. The surface exposed regions of gp29.2 and gp2.7 make SPO1 of interest as a nanocage for phage display. Our findings advance the understanding of capsid architecture, stabilization, and local curvature determination for SPO1-related bacteriophages. PubMed: 40885197DOI: 10.1016/j.str.2025.08.004 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3 Å) |
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