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2fg4
From Proteopedia
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Structure of Human Ferritin L Chain
Contents |
Overview
Ferritin is the major iron-storage protein present in all cells. It, generally contains 24 subunits, with different ratios of heavy chain (H), to light chain (L), in the shape of a hollow sphere hosting up to 4500, ferric Fe atoms inside. H-rich ferritins catalyse the oxidation of, iron(II), while L-rich ferritins promote the nucleation and storage of, iron(III). Several X-ray structures have been determined, including those, of L-chain ferritins from horse spleen (HoSF), recombinant L-chain, ferritins from horse (HoLF), mouse (MoLF) and bullfrog (BfLF) as well as, recombinant human H-chain ferritin (HuHF). Here, structures have been, determined of two crystal forms of recombinant human L-chain ferritin, (HuLF) obtained from native and perdeuterated proteins. The structures, show a cluster of acidic residues at the ferrihydrite nucleation site and, at the iron channel along the threefold axis. An ordered Cd2+ structure is, observed within the iron channel, offering further insight into the route, and mechanism of iron transport into the capsid. The loop between helices, D and E, which is disordered in many other L-chain structures, is clearly, visible in these two structures. The crystals generated from perdeuterated, HuLF will be used for neutron diffraction studies.
Disease
Known diseases associated with this structure: Basal ganglia disease, adult-onset OMIM:[134790], Hyperferritinemia-cataract syndrome OMIM:[134790]
About this Structure
2FG4 is a Single protein structure of sequence from Homo sapiens with CD as ligand. Full crystallographic information is available from OCA.
Reference
Structure of human ferritin L chain., Wang Z, Li C, Ellenburg M, Soistman E, Ruble J, Wright B, Ho JX, Carter DC, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):800-6. Epub 2006, Jun 20. PMID:16790936
Page seeded by OCA on Mon Nov 12 22:04:51 2007
