9CLT

Transferrin Binding Protein A in complex with transferrin binding protein B and transferrin (iron bound to N lobe only)

9CLT の概要

• エントリーDOI: 10.2210/pdb9clt/pdb
• EMDBエントリー: 45730
• 分子名称: Transferrin-binding protein A, Transferrin-binding protein B, Transferrin, ... (5 entities in total)
• 機能のキーワード: membrane protein, metal transporter, iron import, ton b-dependent transporter, transport protein
• 由来する生物種: Neisseria meningitidis; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 255523.86

構造登録者

Dubey, S.,Noinaj, N. (登録日: 2024-07-12, 公開日: 2026-03-11, 最終更新日: 2026-04-15)

主引用文献

Dubey, S.,Stoudenmire, J.,Bury, G.,Yang, L.,Fan, Z.,Li, P.,Wadhwa, G.,Pushkar, Y.,Gumbart, J.C.,Cornelissen, C.N.,Noinaj, N.
Structural insights into the mechanism underpinning iron piracy in pathogenic Neisseria.
Sci Adv, 12:eaea2470-eaea2470, 2026

PubMed Abstract: The pathogenesis of hinges on the surface proteins TbpA and TbpB, which orchestrate the acquisition of iron from transferrin. TbpB selectively captures iron-loaded transferrin and delivers it to TbpA for iron import. We report a series of cryo-electron microscopy structures of trapped intermediates along the iron acquisition pathway. These structural studies are supported by pulldowns, electron paramagnetic resonance studies, molecular dynamics simulations, and studies in , which show that TbpA mechanically opens the C-lobe of transferrin, triggering iron release. Once iron is removed, TbpB dissociates and undergoes large subunit rearrangements with its C-lobe rebinding at a different interface on transferrin. TonB binding expands the barrel of TbpA, helping displace the plug to open a path for iron import. This also disrupts the interaction of the plug loop with the C1 domain of transferrin, leading to the dissociation of the spent transferrin. Together, our study provides a more complete understanding of metal acquisition systems in and other Gram-negative bacteria.

PubMed: 41931607
DOI: 10.1126/sciadv.aea2470

実験手法

ELECTRON MICROSCOPY (3.6 Å)