3VE1

The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin

3VE1 の概要

• エントリーDOI: 10.2210/pdb3ve1/pdb
• 関連するPDBエントリー: 3VE2
• 分子名称: Transferrin-binding protein 2, Serotransferrin, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: transferrin receptor, iron acquisition, vaccine candidate, protein-protein complex, host pathogen interaction, receptor, transferrin, lipoprotein, outermembrane protein, transport protein
• 由来する生物種: Neisseria meningitidis serogroup B; 詳細
• 細胞内の位置: Cell outer membrane; Lipid-anchor (Probable): Q09057; Secreted: P02787
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 294815.21

構造登録者

Calmettes, C.,Moraes, T.F. (登録日: 2012-01-06, 公開日: 2012-02-22, 最終更新日: 2024-11-27)

主引用文献

Calmettes, C.,Alcantara, J.,Yu, R.H.,Schryvers, A.B.,Moraes, T.F.
The structural basis of transferrin sequestration by transferrin-binding protein B.
Nat.Struct.Mol.Biol., 19:358-360, 2012

PubMed Abstract: Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin.

PubMed: 22343719
DOI: 10.1038/nsmb.2251

実験手法

X-RAY DIFFRACTION (2.956 Å)