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Structure and mechanism of the tripartite ATP-independent periplasmic (TRAP) transporter

Structure and mechanism of the tripartite ATP-independent periplasmic (TRAP) transporter

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2628405514

Structure and mechanism of the tripartite ATP-independent periplasmic (TRAP) transporter

About this item

Full title

Structure and mechanism of the tripartite ATP-independent periplasmic (TRAP) transporter

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2022-02

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

In bacteria and archaea, tripartite ATP-independent periplasmic (TRAP) transporters uptake essential carboxylate- and sulfonate-containing nutrients into the cytoplasm. Unlike other secondary active transporters, TRAP transporters cannot receive their substrates directly, but do so indirectly via a secreted soluble substrate-binding protein. How a...

Alternative Titles

Full title

Structure and mechanism of the tripartite ATP-independent periplasmic (TRAP) transporter

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2628405514

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2628405514

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/2022.02.13.480285