6XGP

YSD1_17 major capsid protein

Summary for 6XGP

• Entry DOI: 10.2210/pdb6xgp/pdb
• Descriptor: YSD1_17 major capsid protein (2 entities in total)
• Functional Keywords: capsid protein, viral protein
• Biological source: Bacteriophage sp.
• Total number of polymer chains: 2
• Total formula weight: 79891.20

Authors

Grinter, R.,Hardy, J.M.,Dunstan, R.,Lithgow, T.J.,Coulibaly, F.J. (deposition date: 2020-06-17, release date: 2020-07-01, Last modification date: 2023-10-18)

Primary citation

Hardy, J.M.,Dunstan, R.A.,Grinter, R.,Belousoff, M.J.,Wang, J.,Pickard, D.,Venugopal, H.,Dougan, G.,Lithgow, T.,Coulibaly, F.
The architecture and stabilisation of flagellotropic tailed bacteriophages.
Nat Commun, 11:3748-3748, 2020

PubMed Abstract: 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.

PubMed: 32719311
DOI: 10.1038/s41467-020-17505-w

Experimental method

X-RAY DIFFRACTION (2.6 Å)