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Title | Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC. |
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Journal, issue, pages | Sci Adv, Vol. 10, Issue 38, Page eado8107, Year 2024 |
Publish date | Sep 20, 2024 |
Authors | Zhu Qiao / Phong Hoa Do / Joshua Yi Yeo / Rya Ero / Zhuowen Li / Liying Zhan / Sandip Basak / Yong-Gui Gao / |
PubMed 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 ...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 , 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. |
External links | Sci Adv / PubMed:39303029 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.0 - 3.5 Å |
Structure data | EMDB-38933, PDB-8y5f: EMDB-38934, PDB-8y5g: EMDB-38935, PDB-8y5h: EMDB-38936, PDB-8y5i: EMDB-60536, PDB-8zx1: |
Chemicals | ChemComp-MG: ChemComp-SPD: ChemComp-HOH: ChemComp-ATP: |
Source |
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Keywords | TRANSPORT PROTEIN / ABC transporter |