6tsa: Difference between revisions

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-'''Unreleased structure'''
-The entry 6tsa is ON HOLD  until Paper Publication
+==Crystal structure of human L ferritin (HuLf) Fe(III)-loaded for 30 minutes==
+<StructureSection load='6tsa' size='340' side='right'caption='[[6tsa]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6tsa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TSA FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6tr9|6tr9]], [[6trz|6trz]], [[6ts0|6ts0]], [[6ts1|6ts1]]</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=6tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tsa OCA], [http://pdbe.org/6tsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tsa RCSB], [http://www.ebi.ac.uk/pdbsum/6tsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tsa ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/FRIL_HUMAN FRIL_HUMAN]] Defects in FTL are the cause of hereditary hyperferritinemia-cataract syndrome (HHCS) [MIM:[http://omim.org/entry/600886 600886]]. It is an autosomal dominant disease characterized by early-onset bilateral cataract. Affected patients have elevated level of circulating ferritin. HHCS is caused by mutations in the iron responsive element (IRE) of the FTL gene.<ref>PMID:20159981</ref>   Defects in FTL are the cause of neurodegeneration with brain iron accumulation type 3 (NBIA3) [MIM:[http://omim.org/entry/606159 606159]]; also known as adult-onset basal ganglia disease. It is a movement disorder with heterogeneous presentations starting in the fourth to sixth decade. It is characterized by a variety of neurological signs including parkinsonism, ataxia, corticospinal signs, mild nonprogressive cognitive deficit and episodic psychosis. It is linked with decreased serum ferritin levels.<ref>PMID:20159981</ref> <ref>PMID:16116125</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/FRIL_HUMAN FRIL_HUMAN]] 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).<ref>PMID:19923220</ref> <ref>PMID:20159981</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner surface of the protein cage with a key role played by some glutamate residues. An atomic resolution view of how the cluster formation develops starting from a (mu 3 -oxo)tris[(mu 2 -glutamato-kappaO:kappaO')](glutamato-kappaO)(diaquo)triiron(III) seed is provided. The results support the idea that iron biomineralization in ferritin is a process initiating at the level of the protein surface, capable of contributing coordination bonds and electrostatic guidance.
-Authors: Pozzi, C., Ciambellotti, S., Turano, P., Mangani, S.
+Iron biomineral growth from the initial nucleation seed in L-ferritin.,Ciambellotti S, Pozzi C, Mangani S, Turano P Chemistry. 2020 Feb 6. doi: 10.1002/chem.202000064. PMID:32027764<ref>PMID:32027764</ref>
-Description: Crystal structure of human L ferritin (HuLf) Fe(III)-loaded for 30 minutes
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6tsa" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Ciambellotti, S]]
 [[Category: Mangani, S]]
-[[Category: Ciambellotti, S]]
+[[Category: Pozzi, C]]
 [[Category: Turano, P]]
-[[Category: Pozzi, C]]
+[[Category: Hulf]]
+[[Category: Human l ferritin]]
+[[Category: Metal binding protein]]