5l35 | pdb_00005l35
Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution
Structural highlights
FunctionPublication Abstract from PubMedThe 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 approximately 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 A 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 beta-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 alpha-helix-to-beta-strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses. Structure of a headful DNA-packaging bacterial virus at 2.9 A resolution by electron cryo-microscopy.,Zhao H, Li K, Lynn AY, Aron KE, Yu G, Jiang W, Tang L Proc Natl Acad Sci U S A. 2017 Mar 20. pii: 201615025. doi:, 10.1073/pnas.1615025114. PMID:28320961[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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