8H89

Capsid of Ralstonia phage GP4

Summary for 8H89

• Entry DOI: 10.2210/pdb8h89/pdb
• EMDB information: 34539
• Descriptor: Major capsid protein, Virion associated protein (2 entities in total)
• Functional Keywords: ralstonia phage gp4, complex, virus
• Biological source: Ralstonia phage GP4; More
• Total number of polymer chains: 18
• Total formula weight: 509755.36

Authors

Liu, H.R.,Chen, W.Y. (deposition date: 2022-10-22, release date: 2022-11-16, Last modification date: 2023-08-30)

Primary citation

Zheng, J.,Chen, W.,Xiao, H.,Yang, F.,Li, X.,Song, J.,Cheng, L.,Liu, H.
A Capsid Structure of Ralstonia solanacearum podoviridae GP4 with a Triangulation Number T = 9.
Viruses, 14:-, 2022

PubMed Abstract: 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.

PubMed: 36366529
DOI: 10.3390/v14112431

Experimental method

ELECTRON MICROSCOPY (3.7 Å)