1qjs: Difference between revisions
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==Overview== | ==Overview== | ||
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, .. | 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. | ||
==About this Structure== | ==About this Structure== | ||
1QJS is a | 1QJS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PO4, CL, NA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: HIA and HIB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: iron metabolism]] | [[Category: iron metabolism]] | ||
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Revision as of 14:58, 5 November 2007
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MAMMALIAN BLOOD SERUM HAEMOPEXIN GLYCOSYLATED-NATIVE PROTEIN AND IN COMPLEX WITH ITS LIGAND HAEM
OverviewOverview
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.
About this StructureAbout this Structure
1QJS is a Single protein structure of sequence from Oryctolagus cuniculus with PO4, CL, NA and HEM as ligands. Structure known Active Sites: HIA and HIB. Full crystallographic information is available from OCA.
ReferenceReference
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
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