6lp5
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Sinonovacula constricta ferritin== | |
| + | <StructureSection load='6lp5' size='340' side='right'caption='[[6lp5]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6lp5]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LP5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LP5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</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://proteopedia.org/fgij/fg.htm?mol=6lp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lp5 OCA], [http://pdbe.org/6lp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6lp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lp5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/D2JIV0_SINCO D2JIV0_SINCO]] 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.[RuleBase:RU361145] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ferritins are ubiquitous iron-binding proteins that are mainly related to iron storage, detoxification and innate immunity. Here, we present the crystal structure of a marine invertebrate ferritin from Sinonovacula constricta at a resolution of 1.98 A. The S. constricta ferritin (ScFer) possessed some structural similarities with vertebrate ferritins, and they shared a well-conserved architecture composed of five alpha-helical bundles that assembled into a cage-like structure with 24-subunits. The structure of ScFer also showed iron binding sites in the 3-fold channel, ferroxidase center, and putative nucleation sites. Further, electrostatic potential calculations suggested that the electrostatic gradient of the 3-fold channel could provide a guidance mechanism for iron entering the ferritin cavity. | ||
| - | + | Crystallographic characterization of ferritin from Sinonovacula constricta.,Su C, Ming T, Wu Y, Jiang Q, Huan H, Lu C, Zhou J, Li Y, Song H, Su X Biochem Biophys Res Commun. 2020 Mar 26;524(1):217-223. doi:, 10.1016/j.bbrc.2020.01.069. Epub 2020 Jan 23. PMID:31983429<ref>PMID:31983429</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Ming, T | + | <div class="pdbe-citations 6lp5" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ferroxidase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ming, T H]] | ||
[[Category: Su, C]] | [[Category: Su, C]] | ||
| - | [[Category: Su, X | + | [[Category: Su, X R]] |
| + | [[Category: Ferritin]] | ||
| + | [[Category: Marine invertebrate]] | ||
| + | [[Category: Metal binding site]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Sinonovacula constricta]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 06:49, 8 April 2020
Structure of Sinonovacula constricta ferritin
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