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8dl0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM structure of the nucleotide-free and open channel A.aeolicus WzmWzt transporter== | |
| + | <StructureSection load='8dl0' size='340' side='right'caption='[[8dl0]], [[Resolution|resolution]] 4.10Å' 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='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/O67181_AQUAE O67181_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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Spellmon | + | <div class="pdbe-citations 8dl0" style="background-color:#fffaf0;"></div> |
| - | [[Category: Zimmer | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aquifex aeolicus VF5]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Spellmon N]] | ||
| + | [[Category: Zimmer J]] | ||
Current revision
CryoEM structure of the nucleotide-free and open channel A.aeolicus WzmWzt transporter
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