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-Structure paper
タイトル | A Capsid Structure of GP4 with a Triangulation Number T = 9. |
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ジャーナル・号・ページ | Viruses, Vol. 14, Issue 11, Year 2022 |
掲載日 | 2022年11月1日 |
著者 | Jing Zheng / Wenyuan Chen / Hao Xiao / Fan Yang / Xiaowu Li / Jingdong Song / Lingpeng Cheng / Hongrong Liu / |
PubMed 要旨 | GP4, a new phage, is a short-tailed phage. Few structures of phages have been resolved to near-atomic resolution until now. Here, we present a 3.7 Å resolution structure of the GP4 head by cryo- ...GP4, a new phage, is a short-tailed phage. Few structures of phages have been resolved to near-atomic resolution until now. Here, we present a 3.7 Å resolution structure of the GP4 head by cryo-electron microscopy (cryo-EM). The GP4 head contains 540 copies of major capsid protein (MCP) gp2 and 540 copies of cement protein (CP) gp1 arranged in an icosahedral shell with a triangulation number T = 9. The structures of gp2 and gp1 show a canonical HK97-like fold and an Ig-like fold, respectively. The trimeric CPs stick on the surface of the head along the quasi-threefold axis of the icosahedron generating a sandwiched three-layer electrostatic complementary potential, thereby enhancing the head stability. The assembly pattern of the GP4 head provides a platform for the further exploration of the interaction between and corresponding phages. |
リンク | Viruses / PubMed:36366529 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 Å |
構造データ | EMDB-34539: Capsid structure of Ralstonia phage GP4 |
由来 |
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キーワード | VIRUS / Ralstonia phage GP4 / Complex |