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==CryoEM structure of the A. aeolicus WzmWzt transporter bound to 3-O-methyl-D-mannose== | |||
<StructureSection load='8dn8' size='340' side='right'caption='[[8dn8]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8dn8]] 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=8DN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DN8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U90:3-O-methyl-alpha-D-mannopyranose'>U90</scene></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=8dn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dn8 OCA], [https://pdbe.org/8dn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dn8 RCSB], [https://www.ebi.ac.uk/pdbsum/8dn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dn8 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 8dn8" style="background-color:#fffaf0;"></div> | ||
[[Category: Zimmer | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus VF5]] | |||
[[Category: Large Structures]] | |||
[[Category: Spellmon N]] | |||
[[Category: Zimmer J]] | |||
Revision as of 10:49, 21 September 2022
CryoEM structure of the A. aeolicus WzmWzt transporter bound to 3-O-methyl-D-mannoseCryoEM structure of the A. aeolicus WzmWzt transporter bound to 3-O-methyl-D-mannose
Structural highlights
FunctionPublication Abstract from PubMedO 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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