7N88

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

7N88 の概要

• エントリーDOI: 10.2210/pdb7n88/pdb
• EMDBエントリー: 24233
• 分子名称: Lactoferrin-binding protein B, Lactotransferrin, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: lactoferrin, lipoprotein, neisseria, iron import, membrane protein, membrane protein-transport protein complex, membrane protein/transport protein
• 由来する生物種: Neisseria gonorrhoeae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 154929.72

構造登録者

Yadav, R.,Noinaj, N. (登録日: 2021-06-14, 公開日: 2021-12-01, 最終更新日: 2025-05-14)

主引用文献

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

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: 34751649
DOI: 10.7554/eLife.71683

実験手法

ELECTRON MICROSCOPY (3.7 Å)