8y5h
From Proteopedia
Cryo-EM structure of E.coli spermidine transporter PotD-PotABC in pre-translocation state
Structural highlights
FunctionA0A1Q6AZ03_ECOLX Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.[RuleBase:RU364083] Publication Abstract from PubMedPolyamines, 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. 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 Sci Adv. 2024 Sep 20;10(38):eado8107. doi: 10.1126/sciadv.ado8107. Epub 2024 Sep , 20. PMID:39303029[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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