1r03

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[[Image:1r03.gif|left|200px]]<br /><applet load="1r03" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r03.gif|left|200px]]
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caption="1r03, resolution 1.70&Aring;" />
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'''crystal structure of a human mitochondrial ferritin'''<br />
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{{Structure
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|PDB= 1r03 |SIZE=350|CAPTION= <scene name='initialview01'>1r03</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''crystal structure of a human mitochondrial ferritin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1R03 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=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R03 OCA].
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1R03 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R03 OCA].
==Reference==
==Reference==
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Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala., Langlois d'Estaintot B, Santambrogio P, Granier T, Gallois B, Chevalier JM, Precigoux G, Levi S, Arosio P, J Mol Biol. 2004 Jul 2;340(2):277-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15201052 15201052]
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Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala., Langlois d'Estaintot B, Santambrogio P, Granier T, Gallois B, Chevalier JM, Precigoux G, Levi S, Arosio P, J Mol Biol. 2004 Jul 2;340(2):277-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15201052 15201052]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: iron storage; ferritin; x-ray crystallography]]
[[Category: iron storage; ferritin; x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:02 2008''

Revision as of 11:45, 20 March 2008


PDB ID 1r03

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



crystal structure of a human mitochondrial ferritin


Overview

Mitochondrial ferritin is a recently identified protein precursor encoded by an intronless gene. It is specifically taken up by the mitochondria and processed to a mature protein that assembles into functional ferritin shells. The full mature recombinant protein and its S144A mutant were produced to study structural and functional properties. They yielded high quality crystals from Mg(II) solutions which diffracted up to 1.38 Angstrom resolution. The 3D structures of the two proteins resulted very similar to that of human H-ferritin, to which they have high level of sequence identity (approximately 80%). Metal-binding sites were identified in the native crystals and in those soaked in Mn(II) and Zn(II) solutions. The ferroxidase center binds binuclear iron at the sites A and B, and the structures showed that the A site was always fully occupied by Mg(II), Mn(II) or Zn(II), while the occupancy of the B site was variable. In addition, distinct Mg(II) and Zn(II)-binding sites were found in the 3-fold axes to block the hydrophilic channels. Other metal-binding sites, never observed before in H-ferritin, were found on the cavity surface near the ferroxidase center and near the 4-fold axes. Mitochondrial ferritin showed biochemical properties remarkably similar to those of human H-ferritin, except for the difficulty in renaturing to yield ferritin shells and for a reduced ( approximately 41%) rate in ferroxidase activity. This was partially rescued by the substitution of the bulkier Ser144 with Ala, which occurs in H-ferritin. The residue is exposed on a channel that connects the ferroxidase center with the cavity. The finding that the mutation increased both catalytic activity and the occupancy of the B site demonstrated that the channel is functionally important. In conclusion, the present data define the structure of human mitochondrial ferritin and provide new data on the iron pathways within the H-type ferritin shell.

About this Structure

1R03 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala., Langlois d'Estaintot B, Santambrogio P, Granier T, Gallois B, Chevalier JM, Precigoux G, Levi S, Arosio P, J Mol Biol. 2004 Jul 2;340(2):277-93. PMID:15201052

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