8DN8
CryoEM structure of the A. aeolicus WzmWzt transporter bound to 3-O-methyl-D-mannose
Summary for 8DN8
| Entry DOI | 10.2210/pdb8dn8/pdb |
| EMDB information | 27556 |
| Descriptor | ABC transporter, Transport permease protein, 3-O-methyl-alpha-D-mannopyranose (3 entities in total) |
| Functional Keywords | o antigen abc transporter, 3-o-methyl-d-mannose, translocase |
| Biological source | Aquifex aeolicus More |
| Total number of polymer chains | 4 |
| Total formula weight | 153012.93 |
| Authors | Spellmon, N.,Zimmer, J. (deposition date: 2022-07-10, release date: 2022-09-21, Last modification date: 2024-06-12) |
| Primary citation | Spellmon, N.,Muszynski, A.,Gorniak, I.,Vlach, J.,Hahn, D.,Azadi, P.,Zimmer, J. Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter. Nat Commun, 13:5226-5226, 2022 Cited by PubMed Abstract: 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. PubMed: 36064941DOI: 10.1038/s41467-022-32597-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
Download full validation report
