1FHA: Solving The Structure Of Human H Ferritin By Genetically Engineering Intermolecular Crystal Contacts

Citation:
Abstract
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.
PDB ID: 1FHADownload
MMDB ID: 56127
PDB Deposition Date: 1990/12/20
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 1FHA: 24-meric; determined by author and by software (PISA,PQS)
Molecular Components in 1FHA
Label Count Molecule
Proteins (24 molecules)
24
Ferritin(Gene symbol: FTH1)
Molecule annotation
Chemicals (70 molecules)
1
24
2
46
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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