A proposed structure of the prolate phage T4 prehead core

Engel, Andréas; Driel, Roel van; Driedonks, R. A.

doi:10.1016/s0022-5320(82)80028-2

Cited by 21 publications

(14 citation statements)

References 25 publications

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“…The main core protein, gp22, is a highly charged (pI = 4.3), predominantly h helical protein, and is predicted to form a three-stranded coiled-coil structure [121]. gp22 can self-assemble in vitro into filamentous ribbons [122,123]. The core has been proposed to contain from 6 to 10 such ribbons arranged in a helical configuration [123][124][125].…”

Section: Prolate Scaffolding Corementioning

confidence: 99%

“…gp22 can self-assemble in vitro into filamentous ribbons [122,123]. The core has been proposed to contain from 6 to 10 such ribbons arranged in a helical configuration [123][124][125]. Scanning transmission EM observations of the ribbons suggest that gp22 exhibits an elongated rodlike shape [122,123].…”

Section: Prolate Scaffolding Corementioning

confidence: 99%

“…The core has been proposed to contain from 6 to 10 such ribbons arranged in a helical configuration [123][124][125]. Scanning transmission EM observations of the ribbons suggest that gp22 exhibits an elongated rodlike shape [122,123]. The apparently odd mismatch between the sixfold symmetry of the core and the fivefold symmetric shell may function in a kind of Vernier mechanism for length determination of the head [118,125].…”

Section: Prolate Scaffolding Corementioning

confidence: 99%

“…(The T4 core, of course, also contains several other proteins in addition to the main scaffolding protein gp22.) Interestingly, the main protein of the T4 core, gp22, seems to share several structural properties with the scaffolding core proteins of the P22-like phages [121,123]. In contrast to the internal scaffolding cores, the external scaffolds of P4 and X174 both do display strict icosahedral order.…”

Section: Structures Of Scaffolds and Scaffolding Proteinsmentioning

confidence: 99%

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Scaffolding proteins and their role in viral assembly

Dokland

1999

Cellular and Molecular Life Sciences (CMLS)

135

139

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Scaffolding proteins are proteins that are required to catalyse, regulate or modulate some step in the assembly of a macromolecular complex. They associate specifically with the nascent protein complex during assembly, but are subsequently removed, and are absent from the mature structure. Scaffolding proteins have been described primarily from viral systems, in particular from the double-stranded DNA bacteriophages, but most likely play a more general role in macromolecular assembly, a fundamental process in all biological systems. Scaffolding proteins may act in a specific fashion, by actively encouraging the formation of correct protein-protein interactions, or more generally by nucleating and promoting assembly. They may also work to ensure the fidelity of the assembly process by preventing the formation of improper interactions, in many ways similar to the role of molecular chaperones in protein folding. In viruses, scaffolding proteins are found both in the form of internal cores and external bracing, and may form elaborate and complex structures. This review will focus on the viral scaffolding proteins, for which an increasing amount of structural and functional information has recently become available.

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Section: Prolate Scaffolding Corementioning

confidence: 99%

Section: Prolate Scaffolding Corementioning

confidence: 99%

Section: Prolate Scaffolding Corementioning

confidence: 99%

Section: Structures Of Scaffolds and Scaffolding Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

Scaffolding proteins and their role in viral assembly

Dokland

1999

Cellular and Molecular Life Sciences (CMLS)

135

139

View full text Add to dashboard Cite

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“…Such a model was proposed for the major scaffolding protein of bacteriophage T4, which appears to form a set of six intertwined helical chains that extend down the long axis of the prolate T4 capsid (Paulson & Laemmli, 1977;Engel et al, 1982). The symmetry mismatch between the T4 shell and scaffold may be used as a Vernier mechanism to set the T4 length (Paulson & Laemmli, 1977;Kellenberger, 1990).…”

Section: Non-icosahedral Modelsmentioning

confidence: 99%