Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.

ABSTRACT: Uptake of nucleobases and ascorbate is an essential process in all living organisms mediated by SLC23 transport proteins. These transmembrane carriers operate via the elevator alternating-access mechanism, and are composed of two rigid domains whose relative motion drives transport. The lack of large conformational changes within these domains suggests that the interdomain-linkers act as flexible tethers. Here, we show that interdomain-linkers are not mere tethers, but have a key regulatory role in dictating the conformational space of the transporter and defining the rotation axis of the mobile transport domain. By resolving a wide inward-open conformation of the SLC23 elevator transporter UraA and combining biochemical studies using a synthetic nanobody as conformational probe with hydro

SUBMITTER: Kuhn BT 

PROVIDER: S-EPMC11362169 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature