3HOL
The Structure of Intact Ap-TbpB (N and C lobes)
Summary for 3HOL
| Entry DOI | 10.2210/pdb3hol/pdb |
| Related | 3HOE |
| Descriptor | TbpB (2 entities in total) |
| Functional Keywords | transferrin receptor, iron acquisition, vaccine, lipoprotein, transport protein |
| Biological source | Actinobacillus pleuropneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 55731.57 |
| Authors | Moraes, T.F.,Yu, R.H.,Schryvers, A.B.,Strynadka, N.C.J. (deposition date: 2009-06-02, release date: 2009-10-06, Last modification date: 2024-10-16) |
| Primary citation | Moraes, T.F.,Yu, R.H.,Strynadka, N.C.,Schryvers, A.B. Insights into the bacterial transferrin receptor: the structure of transferrin-binding protein B from Actinobacillus pleuropneumoniae. Mol.Cell, 35:523-533, 2009 Cited by PubMed Abstract: Pathogenic bacteria from the Neisseriaceae and Pasteurellacea families acquire iron directly from the host iron-binding glycoprotein, transferrin (Tf), in a process mediated by surface receptor proteins that directly bind host Tf, extract the iron, and transport it across the outer membrane. The bacterial Tf receptor is comprised of a surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), both of which are essential for survival in the host. In this study, we report the 1.98 A resolution structure of TbpB from the porcine pathogen Actinobacillus pleuropneumoniae, providing insights into the mechanism of Tf binding and the role of TbpB. A model for the complex of TbpB bound to Tf is proposed. Mutation of a single surface-exposed Phe residue on TbpB within the predicted interface completely abolishes binding to Tf, suggesting that the TbpB N lobe comprises the sole high-affinity binding region for Tf. PubMed: 19716795DOI: 10.1016/j.molcel.2009.06.029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
Download full validation report
