Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli (Q44021128)

29 November 2017

title

Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli (English)

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29 November 2017

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Lih-Wen Deng

1

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29 November 2017

Richard N Perham

series ordinal

2

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29 November 2017

language of work or name

English

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publication date

1 June 2002

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Journal of Molecular Biology

29 November 2017

published in

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29 November 2017

volume

319

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29 November 2017

issue

3

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29 November 2017

page(s)

603-614

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Filamentous phage structure, infection and assembly

29 November 2017

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Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites

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The adsorption protein of filamentous phage fd: assignment of its disulfide bridges and identification of the domain incorporated in the coat

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7 January 2021

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The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p

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Interaction of the globular domains of pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli.

7 January 2021

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Filamentous phage are released from the bacterial membrane by a two-step mechanism involving a short C-terminal fragment of pIII.

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A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd

7 January 2021

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Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability

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7 January 2021

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Identifiers

DOI

10.1016/S0022-2836(02)00260-7

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29 November 2017

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