6j3q | pdb_00006j3q
From Proteopedia
Capsid structure of a freshwater cyanophage Siphoviridae Mic1
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Structural highlights
Publication Abstract from PubMedCyanobacteria are the most abundant photosynthetic microorganisms, the global distribution of which is mainly regulated by the corresponding cyanophages. A systematic screening of water samples in the Lake Chaohu enabled us to isolate a freshwater siphocyanophage that infects Microcystis wesenbergii, thus termed Mic1. Using cryoelectron microscopy, we solved the 3.5-A structure of Mic1 capsid. The major capsid protein gp40 of an HK97-like fold forms two types of capsomers, hexons and pentons. The capsomers interact with each other via the interweaved N-terminal arms of gp40 in addition to a tail-in-mouth joint along the three-fold symmetric axis, resulting in the assembly of capsid in a mortise-and-tenon pattern. The novel-fold cement protein gp47 sticks at the two-fold symmetric axis and further fixes the capsid. These findings provide structural insights into the assembly of cyanophages, and set up a platform to explore the mechanism of specific interactions and co-evolution with cyanobacteria. Capsid Structure of a Freshwater Cyanophage Siphoviridae Mic1.,Jin H, Jiang YL, Yang F, Zhang JT, Li WF, Zhou K, Ju J, Chen Y, Zhou CZ Structure. 2019 Jul 30. pii: S0969-2126(19)30235-7. doi:, 10.1016/j.str.2019.07.003. PMID:31378451[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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