View source for 8dl0


==CryoEM structure of the nucleotide-free and open channel A.aeolicus WzmWzt transporter==
<StructureSection load='8dl0' size='340' side='right'caption='[[8dl0]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dl0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DL0 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]] 4.1&#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=8dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dl0 OCA], [https://pdbe.org/8dl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dl0 RCSB], [https://www.ebi.ac.uk/pdbsum/8dl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dl0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67182_AQUAE O67182_AQUAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
O antigens are ubiquitous protective extensions of lipopolysaccharides in the extracellular leaflet of the Gram-negative outer membrane. Following biosynthesis in the cytosol, the lipid-linked polysaccharide is transported to the periplasm by the WzmWzt ABC transporter. Often, O antigen secretion requires the chemical modification of its elongating terminus, which the transporter recognizes via a carbohydrate-binding domain (CBD). Here, using components from A. aeolicus, we identify the O antigen structure with methylated mannose or rhamnose as its cap. Crystal and cryo electron microscopy structures reveal how WzmWzt recognizes this cap between its carbohydrate and nucleotide-binding domains in a nucleotide-free state. ATP binding induces drastic conformational changes of its CBD, terminating interactions with the O antigen. ATPase assays and site directed mutagenesis reveal reduced hydrolytic activity upon O antigen binding, likely to facilitate polymer loading into the ABC transporter. Our results elucidate critical steps in the recognition and translocation of polysaccharides by ABC transporters.

Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter.,Spellmon N, Muszynski A, Gorniak I, Vlach J, Hahn D, Azadi P, Zimmer J Nat Commun. 2022 Sep 5;13(1):5226. doi: 10.1038/s41467-022-32597-2. PMID:36064941<ref>PMID:36064941</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8dl0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Spellmon N]]
[[Category: Zimmer J]]