8Y5G
Cryo-EM structure of E.coli spermidine transporter PotABC with spermidine
Summary for 8Y5G
Entry DOI | 10.2210/pdb8y5g/pdb |
EMDB information | 38934 |
Descriptor | Spermidine/putrescine import ATP-binding protein PotA, Spermidine/putrescine ABC transporter permease 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 | 4 |
Total formula weight | 140426.30 |
Authors | |
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 Cited by 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: 39303029DOI: 10.1126/sciadv.ado8107 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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