2iu2: Difference between revisions

Revision as of 23:59, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2iu2.png

Template:STRUCTURE 2iu2

RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONSRECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS

Template:ABSTRACT PUBMED 17070541

About this StructureAbout this Structure

2IU2 is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Mon Jul 28 23:59:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2iu2.gif|left|200px]]
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 {{STRUCTURE_2iu2|  PDB=2iu2  |  SCENE=  }}
-'''RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS'''
+===RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17070541}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17070541}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Phosphorylation]]
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