7eel
From Proteopedia
Cyanophage Pam1 capsid asymmetric unit
Structural highlights
Publication Abstract from PubMedDespite previous structural analyses of bacteriophages, quite little is known about the structures and assembly patterns of cyanophages. Using cryo-EM combined with crystallography, we solve the near-atomic-resolution structure of a freshwater short-tailed cyanophage, Pam1, which comprises a 400-A-long tail and an icosahedral capsid of 650 A in diameter. The outer capsid surface is reinforced by trimeric cement proteins with a beta-sandwich fold, which structurally resemble the distal motif of Pam1's tailspike, suggesting its potential role in host recognition. At the portal vertex, the dodecameric portal and connected adaptor, followed by a hexameric needle head, form a DNA ejection channel, which is sealed by a trimeric needle. Moreover, we identify a right-handed rifling pattern that might help DNA to revolve along the wall of the ejection channel. Our study reveals the precise assembly pattern of a cyanophage and lays the foundation to support its practical biotechnological and environmental applications. Structure and assembly pattern of a freshwater short-tailed cyanophage Pam1.,Zhang JT, Yang F, Du K, Li WF, Chen Y, Jiang YL, Li Q, Zhou CZ Structure. 2022 Feb 3;30(2):240-251.e4. doi: 10.1016/j.str.2021.10.004. Epub 2021, Nov 1. PMID:34727518[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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