3HOL

The Structure of Intact Ap-TbpB (N and C lobes)

3HOL の概要

• エントリーDOI: 10.2210/pdb3hol/pdb
• 関連するPDBエントリー: 3HOE
• 分子名称: TbpB (2 entities in total)
• 機能のキーワード: transferrin receptor, iron acquisition, vaccine, lipoprotein, transport protein
• 由来する生物種: Actinobacillus pleuropneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55731.57

構造登録者

Moraes, T.F.,Yu, R.H.,Schryvers, A.B.,Strynadka, N.C.J. (登録日: 2009-06-02, 公開日: 2009-10-06, 最終更新日: 2024-10-16)

主引用文献

Moraes, T.F.,Yu, R.H.,Strynadka, N.C.,Schryvers, A.B.
Insights into the bacterial transferrin receptor: the structure of transferrin-binding protein B from Actinobacillus pleuropneumoniae.
Mol.Cell, 35:523-533, 2009

PubMed Abstract: Pathogenic bacteria from the Neisseriaceae and Pasteurellacea families acquire iron directly from the host iron-binding glycoprotein, transferrin (Tf), in a process mediated by surface receptor proteins that directly bind host Tf, extract the iron, and transport it across the outer membrane. The bacterial Tf receptor is comprised of a surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), both of which are essential for survival in the host. In this study, we report the 1.98 A resolution structure of TbpB from the porcine pathogen Actinobacillus pleuropneumoniae, providing insights into the mechanism of Tf binding and the role of TbpB. A model for the complex of TbpB bound to Tf is proposed. Mutation of a single surface-exposed Phe residue on TbpB within the predicted interface completely abolishes binding to Tf, suggesting that the TbpB N lobe comprises the sole high-affinity binding region for Tf.

PubMed: 19716795
DOI: 10.1016/j.molcel.2009.06.029

実験手法

X-RAY DIFFRACTION (1.98 Å)