8Y5F

Cryo-EM structure of E.coli spermidine transporter PotABC

8Y5F の概要

• エントリーDOI: 10.2210/pdb8y5f/pdb
• EMDBエントリー: 38933
• 分子名称: Spermidine/putrescine import ATP-binding protein PotA, Spermidine/putrescine transport system permease protein PotB, Spermidine/putrescine transport system permease protein PotC (3 entities in total)
• 機能のキーワード: abc transporter, transport protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 147525.29

構造登録者

Qiao, Z.,Gao, Y.G. (登録日: 2024-01-31, 公開日: 2024-10-09)

主引用文献

Qiao, Z.,Do, P.H.,Yeo, J.Y.,Ero, R.,Li, Z.,Zhan, L.,Basak, S.,Gao, Y.G.
Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.
Sci Adv, 10:eado8107-eado8107, 2024

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 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.

PubMed: 39303029
DOI: 10.1126/sciadv.ado8107

実験手法

ELECTRON MICROSCOPY (3.13 Å)