9BCH
Solution structure of the hemoglobin receptor HbpA from Corynebacterium diphtheriae
Summary for 9BCH
| Entry DOI | 10.2210/pdb9bch/pdb |
| NMR Information | BMRB: 31164 |
| Descriptor | Membrane protein (1 entity in total) |
| Functional Keywords | receptor, capping, beta-sandwich, protein binding |
| Biological source | Corynebacterium diphtheriae NCTC 13129 |
| Total number of polymer chains | 1 |
| Total formula weight | 21918.51 |
| Authors | |
| Primary citation | 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 Cited by 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: 39739808DOI: 10.1073/pnas.2411833122 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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