4reu
From Proteopedia
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- | ''' | + | ==Revelation of Endogenously bound Fe2+ ions in the Crystal Structure of Ferritin from Escherichia coli== |
+ | <StructureSection load='4reu' size='340' side='right' caption='[[4reu]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4reu]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4REU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4REU FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='activity'><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 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=4reu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4reu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4reu RCSB], [http://www.ebi.ac.uk/pdbsum/4reu PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Ferritin is an iron regulatory protein. It is responsible for storage and detoxification of excess iron thereby it regulates iron level in the body. Here we report the crystal structure of ferritin with two endogenously expressed Fe atoms binding in both the sites. The protein was purified and characterized by MALDI-TOF and N-terminal amino acid sequencing. The crystal belongs to I4 space group and it diffracted up to 2.5A. The structural analysis suggested that it crystallizes as hexamer and confirmed that it happened to be the first report of endogenously expressed Fe ions incorporated in both the A and B sites, situated in between the helices. | ||
- | + | Revelation of endogenously bound Fe ions in the crystal structure of ferritin from Escherichia coli.,Thiruselvam V, Sivaraman P, Kumarevel T, Ponnuswamy MN Biochem Biophys Res Commun. 2014 Oct 11. pii: S0006-291X(14)01793-8. doi:, 10.1016/j.bbrc.2014.10.007. PMID:25305494<ref>PMID:25305494</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Ferroxidase]] | ||
+ | [[Category: Kumarevel, T S.]] | ||
+ | [[Category: Ponnuswamy, M N.]] | ||
+ | [[Category: Thiruselvam, V.]] | ||
+ | [[Category: Binuclear metal binding]] | ||
+ | [[Category: Ferritin]] | ||
+ | [[Category: Iron-binding]] | ||
+ | [[Category: Oxidoreductase]] |
Revision as of 11:46, 22 October 2014
Revelation of Endogenously bound Fe2+ ions in the Crystal Structure of Ferritin from Escherichia coli
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