4v1w
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==3D structure of horse spleen apoferritin determined by electron cryomicroscopy== | |
| + | <SX load='4v1w' size='340' side='right' viewer='molstar' caption='[[4v1w]], [[Resolution|resolution]] 4.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4v1w]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V1W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.7Å</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=4v1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v1w OCA], [https://pdbe.org/4v1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v1w RCSB], [https://www.ebi.ac.uk/pdbsum/4v1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v1w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Despite recent advances, the structures of many proteins cannot be determined by electron cryomicroscopy because the individual proteins move during irradiation. This blurs the images so that they cannot be aligned with each other to calculate a three-dimensional density. Much of this movement stems from instabilities in the carbon substrates used to support frozen samples in the microscope. Here we demonstrate a gold specimen support that nearly eliminates substrate motion during irradiation. This increases the subnanometer image contrast such that alpha helices of individual proteins are resolved. With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of alpha-helical subunits that is particularly difficult to solve by electron microscopy. This advance in substrate design will enable the solution of currently intractable protein structures. | ||
| - | + | Electron microscopy. Ultrastable gold substrates for electron cryomicroscopy.,Russo CJ, Passmore LA Science. 2014 Dec 12;346(6215):1377-80. doi: 10.1126/science.1259530. PMID:25504723<ref>PMID:25504723</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4v1w" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Equus caballus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Passmore LA]] | ||
| + | [[Category: Russo CJ]] | ||
Current revision
3D structure of horse spleen apoferritin determined by electron cryomicroscopy
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