9BCH

Solution structure of the hemoglobin receptor HbpA from Corynebacterium diphtheriae

9BCH の概要

• エントリーDOI: 10.2210/pdb9bch/pdb
• NMR情報: BMRB: 31164
• 分子名称: Membrane protein (1 entity in total)
• 機能のキーワード: receptor, capping, beta-sandwich, protein binding
• 由来する生物種: Corynebacterium diphtheriae NCTC 13129
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21918.51

構造登録者

Mahoney, B.J.,Clubb, R.T. (登録日: 2024-04-09, 公開日: 2025-01-08)

主引用文献

Mahoney, B.J.,Lyman, L.R.,Ford, J.,Soule, J.,Cheung, N.A.,Goring, A.K.,Ellis-Guardiola, K.,Collazo, M.J.,Cascio, D.,Ton-That, H.,Schmitt, M.P.,Clubb, R.T.
Molecular basis of hemoglobin binding and heme removal in Corynebacterium diphtheriae.
Proc.Natl.Acad.Sci.USA, 122:e2411833122-e2411833122, 2025

PubMed Abstract: To successfully mount infections, nearly all bacterial pathogens must acquire iron, a key metal cofactor that primarily resides within human hemoglobin. causes the life-threatening respiratory disease diphtheria and captures hemoglobin for iron scavenging using the surface-displayed receptor HbpA. Here, we show using X-ray crystallography, NMR, and in situ binding measurements that selectively captures iron-loaded hemoglobin by partially ensconcing the heme molecules of its α subunits. Quantitative growth and heme release measurements are compatible with acquiring heme passively released from hemoglobin's β subunits. We propose a model in which HbpA and heme-binding receptors collectively function on the surface to capture hemoglobin and its spontaneously released heme. Acquisition mechanisms that exploit the propensity of hemoglobin's β subunit to release heme likely represent a common strategy used by bacterial pathogens to obtain iron during infections.

PubMed: 39739808
DOI: 10.1073/pnas.2411833122

実験手法

SOLUTION NMR