8VSI
Mechanistic Insights Revealed by YbtPQ in the Occluded State
Summary for 8VSI
| Entry DOI | 10.2210/pdb8vsi/pdb |
| EMDB information | 43498 |
| Descriptor | ABC transporter ATP-binding protein, Permease and ATP-binding protein of yersiniabactin-iron ABC transporter YbtQ, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | abc importer, siderophore, occluded, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 134011.67 |
| Authors | |
| Primary citation | Hu, W.,Parkinson, C.,Zheng, H. Mechanistic Insights Revealed by YbtPQ in the Occluded State. Biomolecules, 14:-, 2024 Cited by PubMed Abstract: Recently, several ATP-binding cassette (ABC) importers have been found to adopt the typical fold of type IV ABC exporters. Presumably, these importers would function under the transport scheme of "alternating access" like those exporters, cycling through inward-open, occluded, and outward-open conformations. Understanding how the exporter-like importers move substrates in the opposite direction requires structural studies on all the major conformations. To shed light on this, here we report the structure of yersiniabactin importer YbtPQ from uropathogenic in the occluded conformation trapped by ADP-vanadate (ADP-Vi) at a 3.1 Å resolution determined by cryo-electron microscopy. The structure shows unusual local rearrangements in multiple helices and loops in its transmembrane domains (TMDs). In addition, the dimerization of the nucleotide-binding domains (NBDs) promoted by the vanadate trapping is highlighted by the "screwdriver" action at one of the two hinge points. These structural observations are rare and thus provide valuable information to understand the structural plasticity of the exporter-like ABC importers. PubMed: 38540742DOI: 10.3390/biom14030322 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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