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dc.contributor.authorAgnello, Emily
dc.contributor.authorPajak, Joshua
dc.contributor.authorLiu, Xingchen
dc.contributor.authorKelch, Brian A
dc.date.accessioned2023-01-31T20:55:32Z
dc.date.available2023-01-31T20:55:32Z
dc.date.issued2022-10-04
dc.identifier.citationStructure and assembly of an extremely long bacteriophage tail tube Emily Agnello, Joshua Pajak, Xingchen Liu, Brian A Kelch bioRxiv 2022.10.03.510161; doi: https://doi.org/10.1101/2022.10.03.510161en_US
dc.identifier.doi10.1101/2022.10.03.510161en_US
dc.identifier.urihttp://hdl.handle.net/20.500.14038/51616
dc.descriptionThis article is a preprint. Preprints are preliminary reports of work that have not been certified by peer review.en_US
dc.description.abstractTail tube assembly is an essential step in the assembly of long-tailed bacteriophages. Limited structural and biophysical information has impeded an understanding of assembly and stability of their long, flexible tail tubes. The hyperthermophilic phage P74-26 is particularly intriguing as it has the longest tail of any known virus (nearly 1 μm) and is the most stable known phage. Here, we present the structure of the P74-26 tail tube and introduce an in vitro system for studying the kinetics of tube assembly. Our high resolution cryo-EM structure provides insight into how the P74-26 phage achieves its flexibility and thermostability through assembly of flexible loops into neighboring rings through tight “ball-and-socket”-like interactions. Guided by this structure, and in combination with mutational, light scattering, and molecular dynamics simulations data, we propose a model for the assembly of conserved tube-like structures across phage and other entities possessing Tail Tube-like proteins. Our model proposes that formation of a full ring licenses the adoption of a tube elongation-competent conformation among the flexible loops and their corresponding sockets, which is further stabilized by an adjacent ring. Tail assembly is controlled by the cooperative interaction of dynamic intra- and inter-ring contacts. Given the structural conservation among tail tube proteins and tail-like structures, our model can explain the mechanism of high-fidelity assembly of long, stable tubes.en_US
dc.language.isoen_USen_US
dc.publisherCold Spring Harbor Laboratoryen_US
dc.relation.ispartofbioRxiven_US
dc.relation.urlhttps://doi.org/10.1101/2022.10.03.510161en_US
dc.rightsThe copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.; Attribution-NonCommercial-NoDerivatives 4.0 Internationalen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectBiophysicsen_US
dc.subjectbacteriophagesen_US
dc.subjecttail tube assemblyen_US
dc.titleStructure and assembly of an extremely long bacteriophage tail tube [preprint]en_US
dc.typePreprinten_US
dc.source.journaltitlebioRxiv
refterms.dateFOA2023-01-31T20:55:33Z
dc.contributor.departmentBiochemistry and Molecular Biotechnologyen_US
dc.contributor.departmentMorningside Graduate School of Biomedical Sciencesen_US


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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.; Attribution-NonCommercial-NoDerivatives 4.0 International
Except where otherwise noted, this item's license is described as The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.; Attribution-NonCommercial-NoDerivatives 4.0 International