2ffx: Difference between revisions

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[[Image:2ffx.gif|left|200px]]
{{Seed}}
[[Image:2ffx.png|left|200px]]


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{{STRUCTURE_2ffx|  PDB=2ffx  |  SCENE=  }}  
{{STRUCTURE_2ffx|  PDB=2ffx  |  SCENE=  }}  


'''Structure of Human Ferritin L. Chain'''
===Structure of Human Ferritin L. Chain===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16790936}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16790936}}


==Disease==
==Disease==
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[[Category: Wright, B S.]]
[[Category: Wright, B S.]]
[[Category: Human ferritin light chain perdeuterated capsid]]
[[Category: Human ferritin light chain perdeuterated capsid]]
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