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Polar confinement of a macromolecular machine by an SRP-type GTPase

Polar confinement of a macromolecular machine by an SRP-type GTPase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_67f7a6eb4e4646ffa7bf8e9a28cdcc67

Polar confinement of a macromolecular machine by an SRP-type GTPase

About this item

Full title

Polar confinement of a macromolecular machine by an SRP-type GTPase

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2024-07, Vol.15 (1), p.5797-11, Article 5797

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The basal structure of the bacterial flagellum includes a membrane embedded MS-ring (formed by multiple copies of FliF) and a cytoplasmic C-ring (composed of proteins FliG, FliM and FliN). The SRP-type GTPase FlhF is required for directing the initial flagellar protein FliF to the cell pole, but the mechanisms are unclear. Here, we show that FlhF a...

Alternative Titles

Full title

Polar confinement of a macromolecular machine by an SRP-type GTPase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_67f7a6eb4e4646ffa7bf8e9a28cdcc67

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_67f7a6eb4e4646ffa7bf8e9a28cdcc67

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-024-50274-4

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