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9XPF

The structure of sheath and tube proteins of phage Phikz

Summary for 9XPF
Entry DOI10.2210/pdb9xpf/pdb
EMDB information67096
DescriptorPHIKZ029, PHIKZ030 (2 entities in total)
Functional Keywordssheath, tube, viral protein
Biological sourcePseudomonas phage phiKZ
More
Total number of polymer chains24
Total formula weight1324786.79
Authors
Xiao, H.,Peng, Z.,Zhou, J.,Liu, H. (deposition date: 2025-11-16, release date: 2026-02-11, Last modification date: 2026-04-29)
Primary citationXiao, 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, 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: 41974715
DOI: 10.1038/s41467-026-71561-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.15 Å)
Structure validation

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