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| | <StructureSection load='6sht' size='340' side='right'caption='[[6sht]], [[Resolution|resolution]] 2.73Å' scene=''> | | <StructureSection load='6sht' size='340' side='right'caption='[[6sht]], [[Resolution|resolution]] 2.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sht]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SHT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SHT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sht]] 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=6SHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SHT 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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.73Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wnw|3wnw]]</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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fth1, Fth ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6sht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sht OCA], [https://pdbe.org/6sht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sht RCSB], [https://www.ebi.ac.uk/pdbsum/6sht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sht ProSAT]</span></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=6sht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sht OCA], [http://pdbe.org/6sht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sht RCSB], [http://www.ebi.ac.uk/pdbsum/6sht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sht ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FRIH_MOUSE FRIH_MOUSE]] 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.<ref>PMID:19154717</ref> | + | [https://www.uniprot.org/uniprot/FRIH_MOUSE FRIH_MOUSE] 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.<ref>PMID:19154717</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6sht" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6sht" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Hamdi, F]] | + | [[Category: Hamdi F]] |
| - | [[Category: Kastritis, P L]] | + | [[Category: Kastritis PL]] |
| - | [[Category: Kyrilis, F]] | + | [[Category: Kyrilis F]] |
| - | [[Category: Meister, A]] | + | [[Category: Meister A]] |
| - | [[Category: Parthier, C]] | + | [[Category: Parthier C]] |
| - | [[Category: Schmidt, L]] | + | [[Category: Schmidt L]] |
| - | [[Category: Semchonok, D]] | + | [[Category: Semchonok D]] |
| - | [[Category: Skalidis, I]] | + | [[Category: Skalidis I]] |
| - | [[Category: Stubbs, M T]] | + | [[Category: Stubbs MT]] |
| - | [[Category: Tueting, C]] | + | [[Category: Tueting C]] |
| - | [[Category: Apoferritin]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Iron binding]]
| + | |
| - | [[Category: Iron storing]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
FRIH_MOUSE 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.[1]
Publication Abstract from PubMed
Here we present the structure of mouse H-chain apoferritin at 2.7 A (FSC = 0.143) solved by single particle cryogenic electron microscopy (cryo-EM) using a 200 kV device, the Thermo Fisher Glacios(R). This is a compact, two-lens illumination system with a constant power objective lens, without any energy filters or aberration correctors, often thought of as a "screening cryo-microscope". Coulomb potential maps reveal clear densities for main chain carbonyl oxygens, residue side chains (including alternative conformations) and bound solvent molecules. We used a quasi-crystallographic reciprocal space approach to fit model coordinates to the experimental cryo-EM map. We argue that the advantages offered by (a) the high electronic and mechanical stability of the microscope, (b) the high emission stability and low beam energy spread of the high brightness Field Emission Gun (X-FEG), (c) direct electron detection technology and (d) particle-based Contrast Transfer Function (CTF) refinement have contributed to achieving high resolution. Overall, we show that basic electron optical settings for automated cryo-electron microscopy imaging can be used to determine structures approaching atomic resolution.
2.7 A cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope.,Hamdi F, Tuting C, Semchonok DA, Visscher KM, Kyrilis FL, Meister A, Skalidis I, Schmidt L, Parthier C, Stubbs MT, Kastritis PL PLoS One. 2020 May 6;15(5):e0232540. doi: 10.1371/journal.pone.0232540., eCollection 2020. PMID:32374767[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li JY, Paragas N, Ned RM, Qiu A, Viltard M, Leete T, Drexler IR, Chen X, Sanna-Cherchi S, Mohammed F, Williams D, Lin CS, Schmidt-Ott KM, Andrews NC, Barasch J. Scara5 is a ferritin receptor mediating non-transferrin iron delivery. Dev Cell. 2009 Jan;16(1):35-46. doi: 10.1016/j.devcel.2008.12.002. PMID:19154717 doi:http://dx.doi.org/10.1016/j.devcel.2008.12.002
- ↑ Hamdi F, Tuting C, Semchonok DA, Visscher KM, Kyrilis FL, Meister A, Skalidis I, Schmidt L, Parthier C, Stubbs MT, Kastritis PL. 2.7 A cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope. PLoS One. 2020 May 6;15(5):e0232540. doi: 10.1371/journal.pone.0232540., eCollection 2020. PMID:32374767 doi:http://dx.doi.org/10.1371/journal.pone.0232540
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