Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution

Sun, Lei; Zhang, Xinzheng; Gao, Song; Rao, Prashant; Padilla-Sanchez, Victor; Chen, Zhenguo; Sun, Siyang; Xiang, Ye; Subramaniam, Sriram; Rao, Venigalla B.; Rossmann, Michael G.

doi:10.1038/ncomms8548

Cited by 90 publications

(128 citation statements)

References 57 publications

(92 reference statements)

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“…3B and 5) with 12-fold symmetry (SI Appendix, Figs. S7 and S8 and Table S3), similar to other tailed phages (35)(36)(37)(38). The gateway complex has sixfold symmetry ( Fig.…”

Section: Significancesupporting

confidence: 54%

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Nováček

Šiborová

Benešík

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with “double-layered” baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210° rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome’s release.

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“…3B and 5) with 12-fold symmetry (SI Appendix, Figs. S7 and S8 and Table S3), similar to other tailed phages (35)(36)(37)(38). The gateway complex has sixfold symmetry ( Fig.…”

Section: Significancesupporting

confidence: 54%

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Nováček

Šiborová

Benešík

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…The outer shell of the T4 head is formed by 930 copies of the major capsid protein, gene product 23 (gp23), which is organized into a hexagonal lattice characterized by the triangulation numbers T end = 13 laevo for the icosahedral ends and T mid = 20 for the midsection (Fokine et al, 2004). Eleven capsid vertices are occupied by pentamers of the special vertex protein, gp24 (Fokine et al, 2005), whereas the twelfth vertex is occupied by the dodecameric protein, gp20 (Sun et al, 2015), which is a portal for DNA packaging during the capsid assembly and exit during infection.…”

Section: Introductionmentioning

confidence: 99%

Common Evolutionary Origin of Procapsid Proteases, Phage Tail Tubes, and Tubes of Bacterial Type VI Secretion Systems

Fokine

Rossmann

2016

Structure

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SUMMARY Many large viruses, including tailed dsDNA bacteriophages and herpesviruses, assemble their capsids via formation of precursors, called procapsids or proheads. The prohead has an internal core, made of scaffolding proteins, and an outer shell, formed by the major capsid protein. The prohead usually contains a protease which is activated during capsid maturation to destroy the inner core and liberate space for the genome. Here we report a 2.0 Å-resolution structure of the pentameric procapsid protease of bacteriophage T4, gene product (gp)21. The structure corresponds to the enzyme’s pre-active state in which its N-terminal region blocks the catalytic center, demonstrating that the activation mechanism involves self-cleavage of nine N-terminal residues. We describe similarities and differences between T4 gp21 and related herpesvirus proteases. We found that gp21 and the herpesvirus proteases have similarity with proteins forming the tubes of phage tails and bacterial type VI secretion systems, suggesting their common evolutionary origin.

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“…Portal gate closing has been reported in SPP1 (Orlova et al, 2003) and speculated in T4(Sun et al, 2015). Moreover, it was reported that SPP1 portal undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA.…”

Section: Discussionmentioning

confidence: 96%

“…1) (Lebedev et al, 2007; Lhuillier et al, 2009). The T4 portal exists as a dodecameric ring that is 14 nm long and 7 nm wide, and an interior channel of ~3 nm in diameter (Sun et al, 2015). The T3 portal is a mixture of 12 and 13 subunits, depending on the protein expression conditions and other factors.…”

Section: Introductionmentioning

confidence: 99%

Three-step channel conformational changes common to DNA packaging motors of bacterial viruses T3, T4, SPP1, and Phi29

Wang

Yan

et al. 2017

Virology

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The DNA packaging motor of dsDNA bacterial viruses contains a head-tail connector with a channel for genome to enter during assembly and to exit during host infection. The DNA packaging motor of bacterial virus phi29 was recently reported to use the “One-way Revolution” mechanism for DNA packaging. This raises a question of how dsDNA is ejected during infection if the channel acts as a one-way inward valve. Here we report a three step conformational change of the portal channel that is common among DNA translocation motors of bacterial viruses T3, T4, SPP1, and phi29. The channels of these motors exercise three discrete steps of gating, as revealed by electrophysiological assays. It is proposed that the three step channel conformational changes occur during DNA entry process, resulting in a structural transition in preparation of DNA movement in the reverse direction during ejection.

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Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution

Cited by 90 publications

References 57 publications

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Common Evolutionary Origin of Procapsid Proteases, Phage Tail Tubes, and Tubes of Bacterial Type VI Secretion Systems

Three-step channel conformational changes common to DNA packaging motors of bacterial viruses T3, T4, SPP1, and Phi29

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