7JRD
The crystal structure of lactoferrin binding protein B (LbpB) from Neisseria meningitidis in complex with human lactoferrin
Summary for 7JRD
| Entry DOI | 10.2210/pdb7jrd/pdb |
| Descriptor | Lactoferrin-binding protein B, Lactotransferrin, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | lactoferrin binding protein b, neisseria, iron scavenging, lactoferrin, transport protein, metal transport |
| Biological source | Neisseria meningitidis serogroup B More |
| Total number of polymer chains | 2 |
| Total formula weight | 157479.00 |
| Authors | Yadav, R.,Noinaj, N. (deposition date: 2020-08-12, release date: 2021-10-13, Last modification date: 2024-11-20) |
| Primary citation | Yadav, R.,Govindan, S.,Daczkowski, C.,Mesecar, A.,Chakravarthy, S.,Noinaj, N. Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis. Elife, 10:-, 2021 Cited by PubMed Abstract: Lactoferrin-binding protein B (LbpB) is a lipoprotein present on the surface of that has been postulated to serve dual functions during pathogenesis in both iron acquisition from lactoferrin (Lf), and in providing protection against the cationic antimicrobial peptide lactoferricin (Lfcn). While previous studies support a dual role for LbpB, exactly how these ligands interact with LbpB has remained unknown. Here, we present the structures of LbpB from and in complex with human holo-Lf, forming a 1:1 complex and confirmed by size-exclusion chromatography small-angle X-ray scattering. LbpB consists of N- and C-lobes with the N-lobe interacting extensively with the C-lobe of Lf. Our structures provide insight into LbpB's preference towards holo-Lf, and our mutagenesis and binding studies show that Lf and Lfcn bind independently. Our studies provide the molecular details for how LbpB serves to capture and preserve Lf in an iron-bound state for delivery to the membrane transporter LbpA for iron piracy, and as an antimicrobial peptide sink to evade host immune defenses. PubMed: 34751649DOI: 10.7554/eLife.71683 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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