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Architecture of the flexible tail tube of bacteriophage SPP1

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 tub...

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Autores principales: Zinke, Maximilian, Sachowsky, Katrin A. A., Öster, Carl, Zinn-Justin, Sophie, Ravelli, Raimond, Schröder, Gunnar F., Habeck, Michael, Lange, Adam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7666168/
https://www.ncbi.nlm.nih.gov/pubmed/33188213
http://dx.doi.org/10.1038/s41467-020-19611-1
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author Zinke, Maximilian
Sachowsky, Katrin A. A.
Öster, Carl
Zinn-Justin, Sophie
Ravelli, Raimond
Schröder, Gunnar F.
Habeck, Michael
Lange, Adam
author_facet Zinke, Maximilian
Sachowsky, Katrin A. A.
Öster, Carl
Zinn-Justin, Sophie
Ravelli, Raimond
Schröder, Gunnar F.
Habeck, Michael
Lange, Adam
author_sort Zinke, Maximilian
collection PubMed
description 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.
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spelling pubmed-76661682020-11-17 Architecture of the flexible tail tube of bacteriophage SPP1 Zinke, Maximilian Sachowsky, Katrin A. A. Öster, Carl Zinn-Justin, Sophie Ravelli, Raimond Schröder, Gunnar F. Habeck, Michael Lange, Adam Nat Commun Article 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. Nature Publishing Group UK 2020-11-13 /pmc/articles/PMC7666168/ /pubmed/33188213 http://dx.doi.org/10.1038/s41467-020-19611-1 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Zinke, Maximilian
Sachowsky, Katrin A. A.
Öster, Carl
Zinn-Justin, Sophie
Ravelli, Raimond
Schröder, Gunnar F.
Habeck, Michael
Lange, Adam
Architecture of the flexible tail tube of bacteriophage SPP1
title Architecture of the flexible tail tube of bacteriophage SPP1
title_full Architecture of the flexible tail tube of bacteriophage SPP1
title_fullStr Architecture of the flexible tail tube of bacteriophage SPP1
title_full_unstemmed Architecture of the flexible tail tube of bacteriophage SPP1
title_short Architecture of the flexible tail tube of bacteriophage SPP1
title_sort architecture of the flexible tail tube of bacteriophage spp1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7666168/
https://www.ncbi.nlm.nih.gov/pubmed/33188213
http://dx.doi.org/10.1038/s41467-020-19611-1
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