8qcz
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the outward-facing heme-bound FLVCR2== | |
| - | + | <StructureSection load='8qcz' size='340' side='right'caption='[[8qcz]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8qcz]] is a 1 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=8QCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QCZ 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]] 3.1Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8qcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qcz OCA], [https://pdbe.org/8qcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qcz RCSB], [https://www.ebi.ac.uk/pdbsum/8qcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qcz ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/FLVC2_HUMAN FLVC2_HUMAN] Fowler vasculopathy. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLVC2_HUMAN FLVC2_HUMAN] Putative heme b importer/sensor involved in heme homeostasis in response to the metabolic state of the cell and to diet. May act as a sensor of cytosolic and/or mitochondrial heme levels to regulate mitochondrial respiration processes, ATP synthesis and thermogenesis. At low heme levels, interacts with components of electron transfer chain (ETC) complexes and ATP2A2, leading to ubiquitin-mediated degradation of ATP2A2 and inhibition of thermogenesis. Upon heme binding, dissociates from ETC complexes to allow switching from mitochondrial ATP synthesis to thermogenesis. Alternatively, in coordination with ATP2A2 may mediate calcium transport and signaling in response to heme.<ref>PMID:20823265</ref> <ref>PMID:32973183</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Safarian S]] | ||
| + | [[Category: Weng T-H]] | ||
| + | [[Category: Wu D]] | ||
Current revision
Cryo-EM structure of the outward-facing heme-bound FLVCR2
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