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The architecture and stabilisation of flagellotropic tailed bacteriophages
- Source :
- Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020), Nature Communications
- Publication Year :
- 2021
- Publisher :
- Apollo - University of Cambridge Repository, 2021.
-
Abstract
- Funder: Sir Henry Wellcome Fellow (106077/Z/14/Z)<br />Funder: Australian Research Council Laureate Fellow (FL130100038)<br />Flagellotropic bacteriophages engage flagella to reach the bacterial surface as an effective means to increase the capture radius for predation. Structural details of these viruses are of great interest given the substantial drag forces and torques they face when moving down the spinning flagellum. We show that the main capsid and auxiliary proteins form two nested chainmails that ensure the integrity of the bacteriophage head. Core stabilising structures are conserved in herpesviruses suggesting their ancestral origin. The structure of the tail also reveals a robust yet pliable assembly. Hexameric rings of the tail-tube protein are braced by the N-terminus and a β-hairpin loop, and interconnected along the tail by the splayed β-hairpins. By contrast, we show that the β-hairpin has an inhibitory role in the tail-tube precursor, preventing uncontrolled self-assembly. Dyads of acidic residues inside the tail-tube present regularly-spaced motifs well suited to DNA translocation into bacteria through the tail.
- Subjects :
- 0301 basic medicine
145
Science
Amino Acid Motifs
Phage biology
General Physics and Astronomy
Flagellum
Protein Structure, Secondary
General Biochemistry, Genetics and Molecular Biology
631/326/596/432
Bacteriophage
82/80
03 medical and health sciences
chemistry.chemical_compound
Protein structure
Viral genetics
Dna genetics
631/45/535/1258
Electron microscopy
Bacteriophages
lcsh:Science
Herpesviridae
Multidisciplinary
030102 biochemistry & molecular biology
biology
82/16
Chemistry
101/28
Virion
article
DNA
General Chemistry
Virus structures
biology.organism_classification
Dna translocation
Vitrification
030104 developmental biology
Capsid
Flagella
631/326/596/2148
DNA, Viral
Biophysics
Capsid Proteins
lcsh:Q
Protein Multimerization
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020), Nature Communications
- Accession number :
- edsair.doi.dedup.....59136dc5e51d5789a821edc09d3cddee
- Full Text :
- https://doi.org/10.17863/cam.73414