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2fg8

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(New page: 200px<br /> <applet load="2fg8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fg8, resolution 2.50&Aring;" /> '''Structure of Human ...)
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<applet load="2fg8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2fg8, resolution 2.50&Aring;" />
'''Structure of Human Ferritin L Chain'''<br />
'''Structure of Human Ferritin L Chain'''<br />
==Overview==
==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.
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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2FG8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FG8 OCA].
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2FG8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CS:'>CS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FG8 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Carter, D.C.]]
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[[Category: Carter, D C.]]
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[[Category: Ellenburg, M.P.]]
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[[Category: Ellenburg, M P.]]
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[[Category: Ho, J.X.]]
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[[Category: Ho, J X.]]
[[Category: Li, C.]]
[[Category: Li, C.]]
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[[Category: Ruble, J.R.]]
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[[Category: Ruble, J R.]]
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[[Category: Wang, Z.M.]]
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[[Category: Wang, Z M.]]
[[Category: CS]]
[[Category: CS]]
[[Category: ferritin light chain perdeuterated]]
[[Category: ferritin light chain perdeuterated]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:04:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:02 2008''

Revision as of 15:21, 21 February 2008


2fg8, resolution 2.50Å

Drag the structure with the mouse to rotate

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

2FG8 is a Single protein structure of sequence from Homo sapiens with 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

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