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TitleArchitecture of the flexible tail tube of bacteriophage SPP1.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5759, Year 2020
Publish dateNov 13, 2020
AuthorsMaximilian Zinke / Katrin A A Sachowsky / Carl Öster / Sophie Zinn-Justin / Raimond Ravelli / Gunnar F Schröder / Michael Habeck / Adam Lange /
PubMed AbstractBacteriophage 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 ...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.
External linksNat Commun / PubMed:33188213 / PubMed Central
MethodsEM (helical sym.) / NMR (solid-state)
Resolution4.0 Å
Structure data

10792

6yeg

6yq5

EMDB-10792, PDB-6yeg:
Hybrid structure of the SPP1 tail tube by solid-state NMR and cryo EM - Final EM Refinement
PDB-6yq5: Hybrid structure of the SPP1 tail tube by solid-state NMR and cryo EM - NMR Ensemble
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • bacillus phage spp1 (virus)
KeywordsVIRAL PROTEIN / complex / tail tube / scaffolding / DNA transport

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