2FG8

Structure of Human Ferritin L Chain

Summary for 2FG8

• Entry DOI: 10.2210/pdb2fg8/pdb
• Related: 2FFX 2FG4
• Descriptor: Ferritin light chain, CESIUM ION (3 entities in total)
• Functional Keywords: ferritin light chain perdeuterated, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 8
• Total formula weight: 160668.94

Authors

Wang, Z.M.,Li, C.,Ellenburg, M.P.,Ruble, J.R.,Ho, J.X.,Carter, D.C. (deposition date: 2005-12-21, release date: 2006-07-04, Last modification date: 2023-08-30)

Primary citation

Wang, Z.,Li, C.,Ellenburg, M.,Soistman, E.,Ruble, J.,Wright, B.,Ho, J.X.,Carter, D.C.
Structure of human ferritin L chain.
ACTA CRYSTALLOGR.,SECT.D, 62:800-806, 2006

PubMed Abstract: 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.

PubMed: 16790936
DOI: 10.1107/S0907444906018294

Experimental method

X-RAY DIFFRACTION (2.5 Å)