8zx1 | pdb_00008zx1

Cryo-EM structure of E.coli spermidine transporter PotABC in nanodisc

spinqualitylabelsall models 8zx1, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8zx1 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A037Y861_ECOLX Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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