symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / entry receptor-mediated virion attachment to host cell / host cell cytoplasm / receptor-mediated virion attachment to host cell / virion attachment to host cell Similarity search - Function
Domain of unknown function DUF3672 / : / Tip attachment protein J, C-terminal receptor binding domain / Tip attachment protein J, Ig-like domain / Tip attachment protein J second Ig-like domain / Domain of unknown function DUF1983 / : / : / Bacteriophage tail tip fiber protein / Tip attachment protein J,FNIII-A domain ...Domain of unknown function DUF3672 / : / Tip attachment protein J, C-terminal receptor binding domain / Tip attachment protein J, Ig-like domain / Tip attachment protein J second Ig-like domain / Domain of unknown function DUF1983 / : / : / Bacteriophage tail tip fiber protein / Tip attachment protein J,FNIII-A domain / Tip attachment protein J / Putative phage tail protein / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold Similarity search - Domain/homology
National Natural Science Foundation of China (NSFC)
32171190
China
Citation
Journal: Structure / Year: 2024 Title: Architecture of the bacteriophage lambda tail. Authors: Chang Wang / Jinsong Duan / Zhiwei Gu / Xiaofei Ge / Jianwei Zeng / Jiawei Wang / Abstract: Bacteriophage lambda has a double-stranded DNA genome and a long, flexible, non-contractile tail encoded by a contiguous block of 11 genes downstream of the head genes. The tail allows host ...Bacteriophage lambda has a double-stranded DNA genome and a long, flexible, non-contractile tail encoded by a contiguous block of 11 genes downstream of the head genes. The tail allows host recognition and delivery of viral DNA from the head shell to the cytoplasm of the infected cell. Here, we present a high-resolution structure of the tail complex of bacteriophage lambda determined by cryoelectron microscopy. Most component proteins of the lambda tail were determined at the atomic scale. The structure sheds light on the molecular organization of the extensively studied tail of bacteriophage lambda.
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