2y3q
From Proteopedia
(Difference between revisions)
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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> | ||
+ | == Function == | ||
+ | [[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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Antonyuk, S V | + | [[Category: Antonyuk, S V]] |
- | [[Category: Hough, M A | + | [[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
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