期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 116, 期 12, 页码 5493-5498出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1811929116
关键词
filamentous virus; cryo-EM structure; symmetry mismatch; single-stranded circular DNA; helical reconstruction
资金
- Ministry of Science and Technology of China [2016YFA0501100]
- National Natural Science Foundation of China [31861143027, 31470721]
- 973 Program [2015CB910102]
- Junior Thousand Talents Program of China
- Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases
- Beijing Advanced Innovation Center for Structural Biology
- joint Natural Science Foundation of China-Israel Science Foundation Grant [2423/18]
The filamentous bacteriophage IKe infects Escherichia coli cells bearing IncN pili. We report the cryo-electron microscopy structure of the micrometer-long IKe viral particle at a resolution of 3.4 angstrom. The major coat protein [protein 8 (p8)] consists of 47 residues that fold into a similar to 68-angstrom-long helix. An atomic model of the coat protein was built. Five p8 helices in a horizontal layer form a pentamer, and symmetrically neighboring p8 layers form a right-handed helical cylinder having a rise per pentamer of 16.77 angstrom and a twist of 38.52 degrees. The inner surface of the capsid cylinder is positively charged and has direct interactions with the encapsulated circular single-stranded DNA genome, which has an electron density consistent with an unusual left-handed helix structure. Similar to capsid structures of other filamentous viruses, strong capsid packing in the IKe particle is maintained by hydrophobic residues. Despite having a different length and large sequence differences from other filamentous phages, pi-pi interactions were found between Tyr9 of one p8 and Trp29 of a neighboring p8 in IKe that are similar to interactions observed in phage M13, suggesting that, despite sequence divergence, overall structural features are maintained.
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