2iu2: Difference between revisions

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[[Image:2iu2.png|left|200px]]
==RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS==
<StructureSection load='2iu2' size='340' side='right' caption='[[2iu2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iu2]] is a 1 chain structure with 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=2IU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IU2 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cei|2cei]], [[2chi|2chi]], [[2cih|2cih]], [[2clu|2clu]], [[2cn6|2cn6]], [[2cn7|2cn7]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iu2 RCSB], [http://www.ebi.ac.uk/pdbsum/2iu2 PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/2iu2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_2iu2|  PDB=2iu2  |  SCENE=  }}
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<ref>PMID:17070541</ref>


===RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_17070541}}
 
==About this Structure==
[[2iu2]] is a 1 chain structure with 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=2IU2 OCA].


==See Also==
==See Also==
*[[Ferritin|Ferritin]]
*[[Ferritin|Ferritin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017070541</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Ferroxidase]]
[[Category: Ferroxidase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 07:27, 29 September 2014

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

Structural highlights

2iu2 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Related:2cei, 2chi, 2cih, 2clu, 2cn6, 2cn7
Activity:Ferroxidase, with EC number 1.16.3.1
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP. High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541 doi:10.1016/j.jmb.2006.10.010

2iu2, resolution 1.80Å

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