Structural highlights
Function
[HEMO_RABIT] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The ubiquitous use of heme in animals poses severe biological and chemical challenges. Free heme is toxic to cells and is a potential source of iron for pathogens. For protection, especially in conditions of trauma, inflammation and hemolysis, and to maintain iron homeostasis, a high-affinity binding protein, hemopexin, is required. Hemopexin binds heme with the highest affinity of any known protein, but releases it into cells via specific receptors. The crystal structure of the heme-hemopexin complex reveals a novel heme binding site, formed between two similar four-bladed beta-propeller domains and bounded by the interdomain linker. The ligand is bound to two histidine residues in a pocket dominated by aromatic and basic groups. Further stabilization is achieved by the association of the two beta-propeller domains, which form an extensive polar interface that includes a cushion of ordered water molecules. We propose mechanisms by which these structural features provide the dual function of heme binding and release.
Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains.,Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, Baker EN Nat Struct Biol. 1999 Oct;6(10):926-31. PMID:10504726[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, Baker EN. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. Nat Struct Biol. 1999 Oct;6(10):926-31. PMID:10504726 doi:http://dx.doi.org/10.1038/13294
