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6m54

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Current revision (10:48, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6m54' size='340' side='right'caption='[[6m54]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='6m54' size='340' side='right'caption='[[6m54]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6m54]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M54 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M54 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6m54]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M54 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fha|2fha]], [[6m52|6m52]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6m54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m54 OCA], [https://pdbe.org/6m54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m54 RCSB], [https://www.ebi.ac.uk/pdbsum/6m54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m54 ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6m54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m54 OCA], [http://pdbe.org/6m54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m54 RCSB], [http://www.ebi.ac.uk/pdbsum/6m54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m54 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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).
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[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cryo-electron microscopy (cryoEM) has become one of the most important approach for structural biology. However, barriers are still there for an increased successful rate, a better resolution and improved efficiency from sample preparation, data collection to image processing. CryoEM sample preparation is one of the bottlenecks with many efforts made recently, including the optimization of supporting substrate (e.g. ultra-thin carbon, graphene, pure gold, 2d crystal of streptavidin, and affinity modification), which was aimed to solve air-water interface problem, or reduce beam induced motion (BIM), or change particle distribution in the grid hole. Here, we report another effort of developing a new supporting substrate, the amorphous nickel-titanium alloy (ANTA) film, for cryoEM sample preparation as a layer of holey supporting film covering on TEM grid. Our investigations showed advantages of ANTA film in comparison with conventional carbon film, including much better electron conductivity and trace non-specific interaction with protein. These advantages yield less BIM and significantly improved particle distribution during cryoEM experiment of human apo-ferritn, thus resulting an improved reconstruction resolution from a reduced number of micrographs and particles. Unlike the pure gold film, the usage of the ANTA film is just same with the carbon film, compatible to conventional automatic cryoEM data collection procedure.
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Amorphous nickel titanium alloy film: A new choice for cryo electron microscopy sample preparation.,Huang X, Zhang L, Wen Z, Chen H, Li S, Ji G, Yin CC, Sun F Prog Biophys Mol Biol. 2020 Oct;156:3-13. doi: 10.1016/j.pbiomolbio.2020.07.009. , Epub 2020 Aug 3. PMID:32758492<ref>PMID:32758492</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6m54" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ferroxidase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, H]]
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[[Category: Chen H]]
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[[Category: Huang, X]]
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[[Category: Huang X]]
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[[Category: Ji, G]]
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[[Category: Ji G]]
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[[Category: Li, S]]
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[[Category: Li S]]
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[[Category: Sun, F]]
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[[Category: Sun F]]
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[[Category: Wen, Z]]
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[[Category: Wen Z]]
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[[Category: Yin, C]]
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[[Category: Yin C]]
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[[Category: Zhang, L]]
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[[Category: Zhang L]]
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[[Category: Apoferritin heavy chain]]
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[[Category: Homo sapien]]
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[[Category: Metal transport]]
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[[Category: Oxidoreductase]]
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Current revision

Human apo ferritin frozen on TEM grid with Amorphous nickel titanium alloy supporting film

PDB ID 6m54

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