Article

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

2021-12-03

Abstract excerpt

<h4>Summary</h4> Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea and provide important uptake routes for many metabolites 1–3 . They consist of three structural domains, a soluble substrate-binding protein (P-domain), and two transmembrane domains (Q- and M-domains) that form a functional unit 4 . While the structures of the P-domains are well-known, an experime...

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Literature Corpus work: 5dae90bf-abe5-5c26-aca3-7ff80f4dfdec
DOI: 10.1101/2021.12.03.471092

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