Structural highlights
Function
TUBE_BPSPP Forms the 160 nm long, sixfold helical, rigid tail tube. Binding to the entry receptor triggers structural rearrangements of the tail tube leading to ejection of the phage DNA into the host.[1] [2] [3] [4]
Publication Abstract from PubMed
Bacteriophage SPP1 is a double-stranded DNA virus of the Siphoviridae family that infects the bacterium Bacillus subtilis. This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, we present the atomic structure of the tail tube of phage SPP1. Our hybrid structure is based on the integration of structural restraints from solid-state nuclear magnetic resonance (NMR) and a density map from cryo-EM. We show that the tail tube protein gp17.1 organizes into hexameric rings that are stacked by flexible linker domains and, thus, form a hollow flexible tube with a negatively charged lumen suitable for the transport of DNA. Additionally, we assess the dynamics of the system by combining relaxation measurements with variances in density maps.
Architecture of the flexible tail tube of bacteriophage SPP1.,Zinke M, Sachowsky KAA, Oster C, Zinn-Justin S, Ravelli R, Schroder GF, Habeck M, Lange A Nat Commun. 2020 Nov 13;11(1):5759. doi: 10.1038/s41467-020-19611-1. PMID:33188213[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ . PMID:17611601
- ↑ . PMID:18786146
- ↑ . PMID:25525268
- ↑ Chaban Y, Lurz R, Brasiles S, Cornilleau C, Karreman M, Zinn-Justin S, Tavares P, Orlova EV. Structural rearrangements in the phage head-to-tail interface during assembly and infection. Proc Natl Acad Sci U S A. 2015 May 19. pii: 201504039. PMID:25991862 doi:http://dx.doi.org/10.1073/pnas.1504039112
- ↑ Zinke M, Sachowsky KAA, Öster C, Zinn-Justin S, Ravelli R, Schröder GF, Habeck M, Lange A. Architecture of the flexible tail tube of bacteriophage SPP1. Nat Commun. 2020 Nov 13;11(1):5759. PMID:33188213 doi:10.1038/s41467-020-19611-1
