Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39303029.
- Also identified by DOI 10.1126/sciadv.ado8107 and PMC identifier 11414716.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Polyamines, characterized by their polycationic nature, are ubiquitously present in all organisms and play numerous cellular functions. Among polyamines, spermidine stands out as the predominant type in both prokaryotic and eukaryotic cells. The PotD-PotABC protein complex in <i>Escherichia coli</i>, belonging to the adenosine triphosphate-binding cassette transporter family, is a spermidine-preferential uptake system. Here, we report structural details of the polyamine uptake system PotD-PotABC in various states. Our analyses reveal distinct "inward-facing" and "outward-facing" conformations of the PotD-PotABC transporter, as well as conformational changes in the "gating" residues (F222, Y223, D226, and K241 in PotB; Y219 and K223 in PotC) controlling spermidine uptake. Therefore, our structural analysis provides insights into how the PotD-PotABC importer recognizes the substrate-binding protein PotD and elucidates molecular insights into the spermidine uptake mechanism of bacteria.
Medical subject headings
- Spermidine
- ATP-Binding Cassette Transporters
- Escherichia coli Proteins
- Escherichia coli