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- Title
Mechanistic Insights Revealed by YbtPQ in the Occluded State.
- Authors
Hu, Wenxin; Parkinson, Chance; Zheng, Hongjin
- 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 Escherichia coli 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.
- Subjects
TRANSMEMBRANE domains; ESCHERICHIA coli; ATP-binding cassette transporters; IMPORTERS; DIMERIZATION; URODYNAMICS
- Publication
Biomolecules (2218-273X), 2024, Vol 14, Issue 3, p322
- ISSN
2218-273X
- Publication type
Article
- DOI
10.3390/biom14030322