8dou

CryoEM structure of the A. aeolicus WzmWzt transporter bound to ADP

spinqualitylabelsall models 8dou, resolution 3.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dou is a 4 chain structure with sequence from Aquifex aeolicus VF5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.54Å Ligands: ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O67181_AQUAE 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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