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TitleCapsid Structure of a Freshwater Cyanophage Siphoviridae Mic1.
Journal, issue, pagesStructure, Vol. 27, Issue 10, Page 1508-11516.e3, Year 2019
Publish dateOct 1, 2019
AuthorsHua Jin / Yong-Liang Jiang / Feng Yang / Jun-Tao Zhang / Wei-Fang Li / Ke Zhou / Jue Ju / Yuxing Chen / Cong-Zhao Zhou /
PubMed AbstractCyanobacteria 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 ...Cyanobacteria 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-Å 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.
External linksStructure / PubMed:31378451
MethodsEM (single particle)
Resolution3.53 Å
Structure data

EMDB-9774, PDB-6j3q:
Capsid structure of a freshwater cyanophage Siphoviridae Mic1
Method: EM (single particle) / Resolution: 3.53 Å

Source
  • microcystis phage mic1 (virus)
KeywordsVIRUS / cyanophage / Siphoviridae / capsid

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