1fha
From Proteopedia
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SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS
Contents |
Overview
Ferritin is important in iron homeostasis. Its twenty-four chains of two, types, H and L, assemble as a hollow shell providing an iron-storage, cavity. Ferritin molecules in cells containing high levels of iron tend to, be rich in L chains, and may have a long-term storage function, whereas, H-rich ferritins are more active in iron metabolism. The molecular basis, for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown, owing to the difficulties in obtaining crystals ordered enough for X-ray, crystallographic analysis. Here we report the three-dimensional structure, of a human ferritin H-chain homopolymer. By genetically engineering a, change in the sequence of the intermolecular contact region, we obtained, crystals isomorphous with the homologous rat L ferritin and of high enough, quality for X-ray diffraction analysis. The X-ray structure of human H, ferritin shows a novel metal site embedded within each of its four-helix, bundles and we suggest that ferroxidase activity associated with this site, accounts for its rapid uptake of iron.
Disease
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[134770]
About this Structure
1FHA is a Single protein structure of sequence from Homo sapiens with FE and CA as ligands. The following page contains interesting information on the relation of 1FHA with [Ferritin and Transferrin]. Full crystallographic information is available from OCA.
Reference
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts., Lawson DM, Artymiuk PJ, Yewdall SJ, Smith JM, Livingstone JC, Treffry A, Luzzago A, Levi S, Arosio P, Cesareni G, et al., Nature. 1991 Feb 7;349(6309):541-4. PMID:1992356
Page seeded by OCA on Mon Nov 12 16:53:15 2007
