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TitleA Capsid Structure of   GP4 with a Triangulation Number T = 9.
Journal, issue, pagesViruses, Vol. 14, Issue 11, Year 2022
Publish dateNov 1, 2022
AuthorsJing Zheng / Wenyuan Chen / Hao Xiao / Fan Yang / Xiaowu Li / Jingdong Song / Lingpeng Cheng / Hongrong Liu /
PubMed AbstractGP4, 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.
External linksViruses / PubMed:36366529 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

34539

8h89

EMDB-34539: Capsid structure of Ralstonia phage GP4
PDB-8h89: Capsid of Ralstonia phage GP4
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • ralstonia phage gp4 (virus)
KeywordsVIRUS / Ralstonia phage GP4 / Complex

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