8Y5I

Cryo-EM structure of E.coli spermidine transporter PotD-PotABC in translocation intermidiate state

Summary for 8Y5I

• Entry DOI: 10.2210/pdb8y5i/pdb
• EMDB information: 38936
• Descriptor: Spermidine/putrescine import ATP-binding protein PotA, Spermidine/putrescine transport system permease protein PotB, Spermidine/putrescine transport system permease protein PotC, ... (6 entities in total)
• Functional Keywords: abc transporter, transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 187467.12

Authors

Qiao, Z.,Gao, Y.G. (deposition date: 2024-01-31, release date: 2024-10-09)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3 Å)