9XPH
The structure of baseplate central region of phage phikz
Summary for 9XPH
| Entry DOI | 10.2210/pdb9xph/pdb |
| EMDB information | 67098 |
| Descriptor | PHIKZ101, PHIKZ174, PHIKZ164, ... (4 entities in total) |
| Functional Keywords | spike, viral protein |
| Biological source | Pseudomonas phage phiKZ More |
| Total number of polymer chains | 13 |
| Total formula weight | 496907.35 |
| Authors | |
| Primary citation | Xiao, H.,Peng, Z.,Zhou, J.,Chen, Y.,Peng, Y.,Tang, Y.,Li, T.,Chen, W.,Huang, S.Y.,Cheng, L.,Liu, H. Structural atlas of the intact jumbo phage phiKZ. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: Jumbo phage phiKZ, a key model for studying phage nucleus formation and bacterial defense mechanisms, possesses a highly complex tail machine that is essential for infection. Here, we present the structural atlas of the intact jumbo phage phiKZ by cryo-EM, thereby identifying 40 constituent proteins and unveiling its modular architecture. The virion, with a length of approximately 360 nm, is comprised of an icosahedral capsid of 2520 polypeptide chains from 11 proteins, and a massive tail machine of over 900 polypeptide chains from 29 proteins. The tail features a unique, multi-layered neck and a highly elaborate baseplate. The neck is reinforced by whisker-like proteins and anchors the contractile tail, which terminates in the baseplate. The baseplate is constituted by a central hub, an inner periphery of interlocking wedge heterotrimers and hexagonal rings, and an outer periphery with a striking hexagonal star configuration. This intricate peripheral region of the baseplate serves as an extended platform for twelve peripheral fibers, which mediate host cell adsorption. Our findings provide a structural framework for understanding jumbo phage assembly and infection, thus contributing to the foundation for future functional studies and rational engineering of these phages for potential therapeutic applications. PubMed: 41974715DOI: 10.1038/s41467-026-71561-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.02 Å) |
Structure validation
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