2y3q

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3q RCSB], [http://www.ebi.ac.uk/pdbsum/2y3q PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3q RCSB], [http://www.ebi.ac.uk/pdbsum/2y3q PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Antonyuk, S V.]]
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[[Category: Antonyuk, S V]]
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[[Category: Hough, M A.]]
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[[Category: Hough, M A]]
[[Category: Metal binding protein]]
[[Category: Metal binding protein]]
[[Category: Redox]]
[[Category: Redox]]

Revision as of 03:33, 25 December 2014

1.55A STRUCTURE OF APO BACTERIOFERRITIN FROM E. COLI

2y3q, resolution 1.55Å

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