3PQS
The crystal structures of porcine pathogen ApH87_TbpB
Summary for 3PQS
| Entry DOI | 10.2210/pdb3pqs/pdb |
| Related | 3PQU |
| Descriptor | transferrin-binding protein, GLYCEROL, CACODYLATE ION, ... (4 entities in total) |
| Functional Keywords | lipoprotein, transferrin receptor, iron acquisition, vaccine candidate, beta barrel, transferrin binding, transferrin, outermembrane, lipid binding protein |
| Biological source | Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae) |
| Total number of polymer chains | 1 |
| Total formula weight | 58871.04 |
| Authors | Calmettes, C.,Moraes, T.F. (deposition date: 2010-11-26, release date: 2011-02-02, Last modification date: 2024-10-16) |
| Primary citation | Calmettes, C.,Yu, R.H.,Silva, L.P.,Curran, D.,Schriemer, D.C.,Schryvers, A.B.,Moraes, T.F. Structural Variations within the Transferrin Binding Site on Transferrin-binding Protein B, TbpB. J.Biol.Chem., 286:12683-12692, 2011 Cited by PubMed Abstract: Pathogenic bacteria acquire the essential element iron through specialized uptake pathways that are necessary in the iron-limiting environments of the host. Members of the Gram-negative Neisseriaceae and Pasteurellaceae families have adapted to acquire iron from the host iron binding glycoprotein, transferrin (Tf), through a receptor complex comprised of transferring-binding protein (Tbp) A and B. Because of the critical role they play in the host, these surface-exposed proteins are invariably present in clinical isolates and thus are considered prime vaccine targets. The specific interactions between TbpB and Tf are essential and ultimately might be exploited to create a broad-spectrum vaccine. In this study, we report the structure of TbpBs from two porcine pathogens, Actinobacillus pleuropneumoniae and suis. Paradoxically, despite a common Tf target, these swine related TbpBs show substantial sequence variation in their Tf-binding site. The TbpB structures, supported by docking simulations, surface plasmon resonance and hydrogen/deuterium exchange experiments with wild-type and mutant TbpBs, explain why there are structurally conserved elements within TbpB homologs despite major sequence variation that are required for binding Tf. PubMed: 21297163DOI: 10.1074/jbc.M110.206102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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