8VSI

Mechanistic Insights Revealed by YbtPQ in the Occluded State

8VSI の概要

• エントリーDOI: 10.2210/pdb8vsi/pdb
• EMDBエントリー: 43498
• 分子名称: ABC transporter ATP-binding protein, Permease and ATP-binding protein of yersiniabactin-iron ABC transporter YbtQ, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: abc importer, siderophore, occluded, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 134011.67

構造登録者

Hu, W.,Parkinson, C.,Zheng, H. (登録日: 2024-01-24, 公開日: 2024-04-10, 最終更新日: 2025-05-14)

主引用文献

Hu, W.,Parkinson, C.,Zheng, H.
Mechanistic Insights Revealed by YbtPQ in the Occluded State.
Biomolecules, 14:-, 2024

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: 38540742
DOI: 10.3390/biom14030322

実験手法

ELECTRON MICROSCOPY (3.1 Å)