5L35

Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution

Summary for 5L35

• Entry DOI: 10.2210/pdb5l35/pdb
• EMDB information: 8314
• Descriptor: Gene 5 protein, CHLORIDE ION (2 entities in total)
• Functional Keywords: phage, sf6, virus
• Biological source: Shigella phage Sf6 (Shigella flexneri bacteriophage VI)
• Total number of polymer chains: 7
• Total formula weight: 319171.33

Authors

Zhao, H.,Tang, L. (deposition date: 2016-08-03, release date: 2017-03-22, Last modification date: 2024-03-06)

Primary citation

Zhao, H.,Li, K.,Lynn, A.Y.,Aron, K.E.,Yu, G.,Jiang, W.,Tang, L.
Structure of a headful DNA-packaging bacterial virus at 2.9 angstrom resolution by electron cryo-microscopy.
Proc. Natl. Acad. Sci. U.S.A., 114:3601-3606, 2017

PubMed Abstract: The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as ∼50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 Å resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon-like intercapsomer joints, and abundant β-sheet-like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic α-helix-to-β-strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.

PubMed: 28320961
DOI: 10.1073/pnas.1615025114

Experimental method

ELECTRON MICROSCOPY (2.89 Å)