Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4

Crowther, R. Anthony; Lenk, Elaine V.; Kikuchi, Yo; King, Jonathan

doi:10.1016/0022-2836(77)90081-x

Cited by 100 publications

(61 citation statements)

References 34 publications

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“…Detailed characterization of structure and mechanism of cell wall recognition is available for baseplate of Myoviridae bacteriophage T4-infecting, Gram-negative Escherichia coli (8,(14)(15)(16)(17)(18). The T4 baseplate has the shape of a semicircular dome in the native state and the shape of a singlelayered, six-pointed star after the contraction (13,(17)(18)(19). T4 attachment to the bacterial cell wall is mediated by short-and long-tail fibers (13,20,21).…”

Section: Significancementioning

confidence: 99%

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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Section: Significancementioning

confidence: 99%

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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“…1). Upon receptor binding, a recognition signal is sent to the baseplate (8)(9)(10)(11), causing the short tail fibers to extend and irreversibly bind to the outer core region of the lipopolysaccharides (12). This binding is followed by contraction of the outer tail sheath (13,14), penetration of the bacterial membrane by the hollow inner tail tube (Fig.…”

mentioning

confidence: 99%

Structure of the bacteriophage T4 long tail fiber receptor-binding tip

Bartual

Otero²,

Garcia-Doval³

et al. 2010

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

172

195

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Bacteriophages are the most numerous organisms in the biosphere. In spite of their biological significance and the spectrum of potential applications, little high-resolution structural detail is available on their receptor-binding fibers. Here we present the crystal structure of the receptor-binding tip of the bacteriophage T4 long tail fiber, which is highly homologous to the tip of the bacteriophage lambda side tail fibers. This structure reveals an unusual elongated sixstranded antiparallel beta-strand needle domain containing seven iron ions coordinated by histidine residues arranged colinearly along the core of the biological unit. At the end of the tip, the three chains intertwine forming a broader head domain, which contains the putative receptor interaction site. The structure reveals a previously unknown beta-structured fibrous fold, provides insights into the remarkable stability of the fiber, and suggests a framework for mutations to expand or modulate receptor-binding specificity.gene product 37 | host cell attachment | octahedral coordination | viral fibers | X-ray crystallography

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“…3 The derivation is found in Appendix A 4 In the Crane's first subassembly process, for example, q = 0.01, M = 1, 000, 000, L = 1, 000, N = 3, and r 1 = r 2 = r 3 = 10. 5 The proof is found in Appendix B which gives N = 6. The corresponding yield is:…”

Section: Models Of Subassembly Processes In Biological Assemblymentioning

confidence: 98%

Subassembly Generation via Mechanical Conformational Switches

Jakiela

1995

Artificial Life

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A question is posed on how a particular subassembly sequence is generated in randomized assembly. An extended design of mechanical conformational switches [16] is proposed, which can encode several subassembly sequences. A particular subassembly sequence is generated due to conformational changes of parts during one-dimensional randomized assembly. The optimal subassembly sequence that maximizes the yield of a desired assembly can be found via genetic search over a space of parameterized conformational switch designs, rather than a space of subassembly sequences. The resulting switch design encodes the optimal subassembly sequence so that the desired assemblies are put together only in the optimal sequence. The results of genetic search and rate equation analyses reveal that the optimal subassembly sequence depends on the initial concentration of parts and the defect probabilities during randomized assembly. The results indicate that abundant parts and parts with high defect probabilities should be assembled earlier rather than later.

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Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4

Cited by 100 publications

References 34 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

Structure of the bacteriophage T4 long tail fiber receptor-binding tip

Subassembly Generation via Mechanical Conformational Switches

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