9CLT
Transferrin Binding Protein A in complex with transferrin binding protein B and transferrin (iron bound to N lobe only)
Summary for 9CLT
| Entry DOI | 10.2210/pdb9clt/pdb |
| EMDB information | 45730 |
| Descriptor | Transferrin-binding protein A, Transferrin-binding protein B, Transferrin, ... (5 entities in total) |
| Functional Keywords | membrane protein, metal transporter, iron import, ton b-dependent transporter, transport protein |
| Biological source | Neisseria meningitidis More |
| Total number of polymer chains | 3 |
| Total formula weight | 255523.86 |
| Authors | Dubey, S.,Noinaj, N. (deposition date: 2024-07-12, release date: 2026-03-11, Last modification date: 2026-04-15) |
| Primary citation | 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 Cited by 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: 41931607DOI: 10.1126/sciadv.aea2470 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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