9IOZ

Structure of the bacteriophage T5 tail tip complex

This is a non-PDB format compatible entry.

Summary for 9IOZ

• Entry DOI: 10.2210/pdb9ioz/pdb
• EMDB information: 60750
• Descriptor: Baseplate tube protein p140, Distal tail protein pb9, Baseplate hub protein pb3 (3 entities in total)
• Functional Keywords: complex, viral protein
• Biological source: Escherichia phage T5; More
• Total number of polymer chains: 12
• Total formula weight: 561733.96

Authors

Peng, Y.N.,Liu, H.R. (deposition date: 2024-07-10, release date: 2024-09-04, Last modification date: 2025-06-18)

Primary citation

Peng, Y.,Tang, H.,Xiao, H.,Chen, W.,Song, J.,Zheng, J.,Liu, H.
Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection.
Int J Mol Sci, 25:-, 2024

PubMed Abstract: T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, we used cryo-electron microscopy (cryo-EM) to determine the structures of mature T5 (a laboratory-adapted, fiberless T5 mutant) and urea-treated empty T5 (lacking the tip complex) at near-atomic resolutions. Atomic models of the head, connector complex, tail tube, and tail tip were built for mature T5, and atomic models of the connector complex, comprising the portal protein pb7, adaptor protein p144, and tail terminator protein p142, were built for urea-treated empty T5. Our findings revealed that the aforementioned proteins did not undergo global conformational changes before and after DNA ejection, indicating that these structural features were conserved among most myophages and siphophages. The present study elucidates the underlying mechanisms of siphophage infection and DNA ejection.

PubMed: 39126049
DOI: 10.3390/ijms25158479

Experimental method

ELECTRON MICROSCOPY (3.9 Å)