Structure of the intact tail machine of Anabaena myophage A-1(L)

Rong-Cheng Yu, Feng Yang, Hong-Yan Zhang, Pu Hou, Kang Du, Jie Zhu, Ning Cui, Xudong Xu, Yuxing Chen, Qiong Li () and Cong-Zhao Zhou ()
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Rong-Cheng Yu: University of Science and Technology of China
Feng Yang: University of Science and Technology of China
Hong-Yan Zhang: University of Science and Technology of China
Pu Hou: University of Science and Technology of China
Kang Du: University of Science and Technology of China
Jie Zhu: University of Science and Technology of China
Ning Cui: University of Science and Technology of China
Xudong Xu: Chinese Academy of Sciences
Yuxing Chen: University of Science and Technology of China
Qiong Li: University of Science and Technology of China
Cong-Zhao Zhou: University of Science and Technology of China

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract The Myoviridae cyanophage A-1(L) specifically infects the model cyanobacteria Anabaena sp. PCC 7120. Following our recent report on the capsid structure of A-1(L), here we present the high-resolution cryo-EM structure of its intact tail machine including the neck, tail and attached fibers. Besides the dodecameric portal, the neck contains a canonical hexamer connected to a unique pentadecamer that anchors five extended bead-chain-like neck fibers. The 1045-Å-long contractile tail is composed of a helical bundle of tape measure proteins surrounded by a layer of tube proteins and a layer of sheath proteins, ended with a five-component baseplate. The six long and six short tail fibers are folded back pairwise, each with one end anchoring to the baseplate and the distal end pointing to the capsid. Structural analysis combined with biochemical assays further enable us to identify the dual hydrolytic activities of the baseplate hub, in addition to two host receptor binding domains in the tail fibers. Moreover, the structure of the intact A-1(L) also helps us to reannotate its genome. These findings will facilitate the application of A-1(L) as a chassis cyanophage in synthetic biology.

Date: 2024
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DOI: 10.1038/s41467-024-47006-z

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