The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions (Q27640645)

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Stacy D Benson

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Dennis H Bamford

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Roger M Burnett

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publication date

March 2003

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published in

Structure

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volume

11

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issue

3

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page(s)

309-22

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cites work

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DNA packaging orders the membrane of bacteriophage PRD1.

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Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions

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Comparison of the Lipid-containing Bacteriophages PRD1, PR3, PR4, PR5 and L17

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The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution

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Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon

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A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly

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A new mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex

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Assembly of a functional phage PRD1 receptor depends on 11 genes of the IncP plasmid mating pair formation complex

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12623018

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Consolidated OpenCitations Corpus – April 2017