6YEG

Hybrid structure of the SPP1 tail tube by solid-state NMR and cryo EM - Final EM Refinement

Summary for 6YEG

• Entry DOI: 10.2210/pdb6yeg/pdb
• Related: 6YQ5
• EMDB information: 10792
• NMR Information: BMRB: 27468
• Descriptor: Tail tube protein gp17.1* (1 entity in total)
• Functional Keywords: complex, tail tube, scaffolding, dna transport, viral protein
• Biological source: Bacillus phage SPP1
• Total number of polymer chains: 12
• Total formula weight: 236093.41

Authors

Zinke, M.,Sachowsky, K.A.A.,Zinn-Justin, S.,Ravelli, R.,Schroder, G.F.,Habeck, M.,Lange, A. (deposition date: 2020-03-24, release date: 2020-10-14, Last modification date: 2023-09-13)

Primary citation

Zinke, M.,Sachowsky, K.A.A.,Oster, C.,Zinn-Justin, S.,Ravelli, R.,Schroder, G.F.,Habeck, M.,Lange, A.
Architecture of the flexible tail tube of bacteriophage SPP1.
Nat Commun, 11:5759-5759, 2020

PubMed Abstract: 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.

PubMed: 33188213
DOI: 10.1038/s41467-020-19611-1

Experimental method

ELECTRON MICROSCOPY (4 Å)
SOLID-STATE NMR (4 Å)