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== | ==recombinant mouse L-chain ferritin== | ||
Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained | <StructureSection load='1h96' size='340' side='right'caption='[[1h96]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1h96]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H96 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h96 OCA], [https://pdbe.org/1h96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h96 RCSB], [https://www.ebi.ac.uk/pdbsum/1h96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h96 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FRIL1_MOUSE FRIL1_MOUSE] 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/1h96_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h96 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature. | |||
Structure of mouse L-chain ferritin at 1.6 A resolution.,Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711<ref>PMID:11679711</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1h96" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Arosio P]] | |||
[[Category: Arosio | [[Category: Beaumont C]] | ||
[[Category: Beaumont | [[Category: Chevalier JM]] | ||
[[Category: Chevalier | [[Category: D'Estaintot BL]] | ||
[[Category: | [[Category: Dautant A]] | ||
[[Category: | [[Category: Gallois B]] | ||
[[Category: Gallois | [[Category: Granier T]] | ||
[[Category: Granier | [[Category: Mellado JM]] | ||
[[Category: Mellado | [[Category: Precigoux G]] | ||
[[Category: Precigoux | [[Category: Santambrogio P]] | ||
[[Category: Santambrogio | |||
Latest revision as of 15:20, 13 December 2023
recombinant mouse L-chain ferritinrecombinant mouse L-chain ferritin
Structural highlights
FunctionFRIL1_MOUSE 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature. Structure of mouse L-chain ferritin at 1.6 A resolution.,Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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