6xgp
YSD1_17 major capsid protein
Structural highlights
FunctionA0A498U580_9CAUD Assembles to form an icosahedral capsid. The assembly is primed by the interaction between capsid assembly protease and portal dodecamer, and major capsid proteins assemble cooperatively to form the procapsid with the help of capsid scaffolding protein. Major capsid protein forms hexons and pentons of the icosahedron. Viral genomic DNA is packaged into the procapsid through the portal vertex. The packaging triggers a dramatic reconfiguration of the capsid shell.[HAMAP-Rule:MF_04133] Publication Abstract from PubMedFlagellotropic 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 beta-hairpin loop, and interconnected along the tail by the splayed beta-hairpins. By contrast, we show that the beta-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. The architecture and stabilisation of flagellotropic tailed bacteriophages.,Hardy JM, Dunstan RA, Grinter R, Belousoff MJ, Wang J, Pickard D, Venugopal H, Dougan G, Lithgow T, Coulibaly F Nat Commun. 2020 Jul 27;11(1):3748. doi: 10.1038/s41467-020-17505-w. PMID:32719311[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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