Architecture of the flexible tail tube of bacteriophage SPP1
| Autor: | Raimond B. G. Ravelli, Adam Lange, Maximilian Zinke, Sophie Zinn-Justin, Michael Habeck, Carl Öster, Katrin A. A. Sachowsky, Gunnar F. Schröder |
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| Přispěvatelé: | Institute of Nanoscopy (IoN), RS: M4I - Nanoscopy, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Enveloppe Nucléaire, Télomères et Réparation de l’ADN (INTGEN), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular DYNAMICS 0301 basic medicine Magnetic Resonance Spectroscopy Materials science Science [SDV]Life Sciences [q-bio] PROTEIN General Physics and Astronomy Bacillus subtilis Siphoviridae 010402 general chemistry Solid-state NMR 01 natural sciences Article Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Viral Proteins 03 medical and health sciences chemistry.chemical_compound Protein structure Cryoelectron microscopy FIBRILS CRYO-EM STRUCTURE Bacteriophages Tube (fluid conveyance) Amino Acid Sequence lcsh:Science Multidisciplinary biology Relaxation (NMR) General Chemistry Nuclear magnetic resonance spectroscopy biology.organism_classification 0104 chemical sciences 030104 developmental biology chemistry NMR-SPECTROSCOPY Biophysics Thermodynamics lcsh:Q ddc:500 Linker SYSTEM DNA |
| Zdroj: | Nature Communications, 11(1):5759. Nature Publishing Group Nature Communications Nature Communications, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩ Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020) Nature Communications 11(1), 5759 (2020). doi:10.1038/s41467-020-19611-1 Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩ |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-020-19611-1 |
| Popis: | 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. Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexible tube formed by hexameric rings stacked by flexible linkers. |
| Databáze: | OpenAIRE |
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