View source for 8zx1


==Cryo-EM structure of E.coli spermidine transporter PotABC in nanodisc==
<StructureSection load='8zx1' size='340' side='right'caption='[[8zx1]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8zx1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZX1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8zx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zx1 OCA], [https://pdbe.org/8zx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zx1 RCSB], [https://www.ebi.ac.uk/pdbsum/8zx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zx1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A037Y861_ECOLX A0A037Y861_ECOLX] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:39303029</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8zx1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Gao YG]]
[[Category: Qiao Z]]