Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.
Sci Adv
; 10(38): eado8107, 2024 Sep 20.
Article
in En
| MEDLINE
| ID: mdl-39303029
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 Escherichia coli, 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Spermidine
/
ATP-Binding Cassette Transporters
/
Escherichia coli Proteins
/
Escherichia coli
Language:
En
Journal:
Sci Adv
Year:
2024
Document type:
Article
Affiliation country:
Singapore
Country of publication:
United States