8vsi

Mechanistic Insights Revealed by YbtPQ in the Occluded State

spinqualitylabelsall models 8vsi, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vsi is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: AOV, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1D7Q186_ECOLX Publication Abstract from PubMed 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 A 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. Mechanistic Insights Revealed by YbtPQ in the Occluded State.,Hu W, Parkinson C, Zheng H Biomolecules. 2024 Mar 8;14(3):322. doi: 10.3390/biom14030322. PMID:38540742 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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