EMD-38934
Cryo-EM structure of E.coli spermidine transporter PotABC with spermidine
EMD-38934
Single-particle3.0 Å
Deposition: 31/01/2024Map released: 09/10/2024
Last modified: 09/10/2024
Sample Organism:
Escherichia coli
Sample: ABC transporter
Fitted models: 8y5g (Avg. Q-score: 0.509)
Deposition Authors: Qiao Z
,
Gao YG
Sample: ABC transporter
Fitted models: 8y5g (Avg. Q-score: 0.509)
Deposition Authors: Qiao Z
,
Gao YG
Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.
Qiao Z ,
Do PH,
Yeo JY ,
Ero R ,
Li Z ,
Zhan L ,
Basak S,
Gao YG
(2024) Sci Adv , 10 , eado8107 - eado8107
,
Do PH,
Yeo JY ,
Ero R ,
Li Z ,
Zhan L ,
Basak S,
Gao YG
(2024) Sci Adv , 10 , eado8107 - eado8107
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.
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.