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Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_120e67d6e4b84738995cb033a43e838a

Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

About this item

Full title

Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-12, Vol.10 (1), p.5567-13, Article 5567

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter cells during cell division. Here, we document binding of syntheti...

Alternative Titles

Full title

Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_120e67d6e4b84738995cb033a43e838a

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_120e67d6e4b84738995cb033a43e838a

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-13354-4

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