TY  - JOUR
AU  - Zinke, Maximilian
AU  - Sachowsky, Katrin A. A.
AU  - Öster, Carl
AU  - Zinn-Justin, Sophie
AU  - Ravelli, Raimond
AU  - Schröder, Gunnar F.
AU  - Habeck, Michael
AU  - Lange, Adam
TI  - Architecture of the flexible tail tube of bacteriophage SPP1
JO  - Nature Communications
VL  - 11
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - FZJ-2021-00348
SP  - 5759
PY  - 2020
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 33188213
UR  - <Go to ISI:>//WOS:000594647500010
DO  - DOI:10.1038/s41467-020-19611-1
UR  - https://juser.fz-juelich.de/record/889727
ER  -