7n88

The cryoEM structure of LbpB from N. gonorrhoeae in complex with lactoferrin

spinqualitylabelsall models 7n88, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7n88 is a 2 chain structure with sequence from Homo sapiens and Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.7Å Ligands: BCT, FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9Z4N2_NEIGO Publication Abstract from PubMed Lactoferrin-binding protein B (LbpB) is a lipoprotein present on the surface of Neisseria 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 N. meningitidis and N. gonorrhoeae 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. Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis.,Yadav R, Govindan S, Daczkowski C, Mesecar A, Chakravarthy S, Noinaj N Elife. 2021 Nov 9;10:e71683. doi: 10.7554/eLife.71683. PMID:34751649 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactoferrin

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