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-Structure paper
タイトル | Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis. |
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ジャーナル・号・ページ | Elife, Vol. 10, Year 2021 |
掲載日 | 2021年11月9日 |
![]() | Ravi Yadav / Srinivas Govindan / Courtney Daczkowski / Andrew Mesecar / Srinivas Chakravarthy / Nicholas Noinaj / ![]() |
PubMed 要旨 | 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), ...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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.85 - 3.7 Å |
構造データ | EMDB-24233, PDB-7n88: ![]() PDB-7jrd: |
化合物 | ![]() ChemComp-SO4: ![]() ChemComp-FE: ![]() ChemComp-BCT: ![]() ChemComp-HOH: |
由来 |
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![]() | METAL TRANSPORT / Lactoferrin binding protein B / Neisseria / iron scavenging / lactoferrin / TRANSPORT PROTEIN / MEMBRANE PROTEIN/TRANSPORT PROTEIN / lipoprotein / iron import / MEMBRANE PROTEIN / MEMBRANE PROTEIN-TRANSPORT PROTEIN complex |