3o7r: Difference between revisions
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==Crystal structure of Ru(p-cymene)/apo-H49AFr== | ==Crystal structure of Ru(p-cymene)/apo-H49AFr== | ||
<StructureSection load='3o7r' size='340' side='right' caption='[[3o7r]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3o7r' size='340' side='right' caption='[[3o7r]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o7s|3o7s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o7s|3o7s]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=3o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7r RCSB], [http://www.ebi.ac.uk/pdbsum/3o7r 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=3o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7r OCA], [http://pdbe.org/3o7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o7r RCSB], [http://www.ebi.ac.uk/pdbsum/3o7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3o7r" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 05:56, 5 August 2016
Crystal structure of Ru(p-cymene)/apo-H49AFrCrystal structure of Ru(p-cymene)/apo-H49AFr
Structural highlights
Function[FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). Publication Abstract from PubMedSpherical protein cages such as an iron storage protein, ferritin, have great potential as nanometer-scale capsules to assemble and store metal ions and complexes. We report herein the synthesis of a composite of an apo-ferritin cage and Ru(p-cymene) complexes. Ru complexes were efficiently incorporated into the ferritin cavity without degradation of its cage structure. X-Ray crystallography revealed that the Ru complexes were immobilized on the interior surface of the cage mainly by the coordination of histidine residues. Incorporation of organometallic Ru complexes into apo-ferritin cage.,Takezawa Y, Bockmann P, Sugi N, Wang Z, Abe S, Murakami T, Hikage T, Erker G, Watanabe Y, Kitagawa S, Ueno T Dalton Trans. 2011 Mar 14;40(10):2190-5. Epub 2010 Nov 26. PMID:21113534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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