2cn7: Difference between revisions
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==Overview== | ==Overview== | ||
Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in the 3-fold axes, 4-fold axes and on the cavity surface near the, ferroxidase centre. To study the importance of the distance of the two, metal atoms in the ferroxidase centre, single and double replacement of, glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal, binding and the correlation with Fe(II) oxidation rates are discussed. | Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in the 3-fold axes, 4-fold axes and on the cavity surface near the, ferroxidase centre. To study the importance of the distance of the two, metal atoms in the ferroxidase centre, single and double replacement of, glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal, binding and the correlation with Fe(II) oxidation rates are discussed. | ||
==Disease== | |||
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134770 134770]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
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Revision as of 22:11, 12 November 2007
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RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT
OverviewOverview
Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in the 3-fold axes, 4-fold axes and on the cavity surface near the, ferroxidase centre. To study the importance of the distance of the two, metal atoms in the ferroxidase centre, single and double replacement of, glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal, binding and the correlation with Fe(II) oxidation rates are discussed.
DiseaseDisease
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[134770]
About this StructureAbout this Structure
2CN7 is a Single protein structure of sequence from Homo sapiens with CA and GOL as ligands. Active as Ferroxidase, with EC number 1.16.3.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541
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