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R pyocin tail fiber structure reveals a receptor-binding domain with a lectin fold

R pyocin tail fiber structure reveals a receptor-binding domain with a lectin fold

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2176240018

R pyocin tail fiber structure reveals a receptor-binding domain with a lectin fold

About this item

Full title

R pyocin tail fiber structure reveals a receptor-binding domain with a lectin fold

Publisher

United States: Public Library of Science

Journal title

PloS one, 2019-02, Vol.14 (2), p.e0211432-e0211432

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

R pyocins are ɸCTX-like myophage tailocins of Pseudomonas sp. Adsorption of R pyocins to target strains occurs by the interaction of tail fiber proteins with core lipopolysaccharide (LPS). Here, we demonstrate that N-terminally truncated R pyocin tail fibers corresponding to a region of variation between R-subtypes are sufficient to bind target str...

Alternative Titles

Full title

R pyocin tail fiber structure reveals a receptor-binding domain with a lectin fold

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_2176240018

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2176240018

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0211432

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