6o58

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<SX load='6o58' size='340' side='right' viewer='molstar' caption='[[6o58]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<SX load='6o58' size='340' side='right' viewer='molstar' caption='[[6o58]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6o58]] is a 16 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=6O58 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O58 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6o58]] is a 16 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=6O58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O58 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=CA:CALCIUM+ION'>CA</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]] 3.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCU, C10orf42, CCDC109A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SMDT1, C22orf32, EMRE ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6o58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o58 OCA], [http://pdbe.org/6o58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o58 RCSB], [http://www.ebi.ac.uk/pdbsum/6o58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o58 ProSAT]</span></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=6o58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o58 OCA], [https://pdbe.org/6o58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o58 RCSB], [https://www.ebi.ac.uk/pdbsum/6o58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o58 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MCU_HUMAN MCU_HUMAN]] Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Activity is regulated by MICU1 and MICU2 that stimulate and inhibit MCU activity, respectively. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes.<ref>PMID:21685886</ref> <ref>PMID:21685888</ref> <ref>PMID:22822213</ref> <ref>PMID:22829870</ref> <ref>PMID:22904319</ref> <ref>PMID:23101630</ref> <ref>PMID:23178883</ref> <ref>PMID:24332854</ref> <ref>PMID:24560927</ref> [[http://www.uniprot.org/uniprot/EMRE_HUMAN EMRE_HUMAN]] Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:24231807, PubMed:26774479, PubMed:27099988). Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU (PubMed:24231807). Plays a central role in regulating the uniplex complex response to intracellular calcium signaling (PubMed:27099988). Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (PubMed:27099988).<ref>PMID:24231807</ref> <ref>PMID:26774479</ref> <ref>PMID:27099988</ref>
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[https://www.uniprot.org/uniprot/MCU_HUMAN MCU_HUMAN] Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Activity is regulated by MICU1 and MICU2 that stimulate and inhibit MCU activity, respectively. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes.<ref>PMID:21685886</ref> <ref>PMID:21685888</ref> <ref>PMID:22822213</ref> <ref>PMID:22829870</ref> <ref>PMID:22904319</ref> <ref>PMID:23101630</ref> <ref>PMID:23178883</ref> <ref>PMID:24332854</ref> <ref>PMID:24560927</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mitochondrial calcium uptake is crucial to the regulation of eukaryotic Ca(2+) homeostasis and is mediated by the mitochondrial calcium uniporter (MCU). While MCU alone can transport Ca(2+) in primitive eukaryotes, metazoans require an essential single membrane-spanning auxiliary component called EMRE to form functional channels; however, the molecular mechanism of EMRE regulation remains elusive. Here, we present the cryo-EM structure of the human MCU-EMRE complex, which defines the interactions between MCU and EMRE as well as pinpoints the juxtamembrane loop of MCU and extended linker of EMRE as the crucial elements in the EMRE-dependent gating mechanism among metazoan MCUs. The structure also features the dimerization of two MCU-EMRE complexes along an interface at the N-terminal domain (NTD) of human MCU that is a hotspot for post-translational modifications. Thus, the human MCU-EMRE complex, which constitutes the minimal channel components among metazoans, provides a framework for future mechanistic studies on MCU.
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Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter.,Wang Y, Nguyen NX, She J, Zeng W, Yang Y, Bai XC, Jiang Y Cell. 2019 May 16;177(5):1252-1261.e13. doi: 10.1016/j.cell.2019.03.050. Epub, 2019 May 9. PMID:31080062<ref>PMID:31080062</ref>
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==See Also==
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*[[Mitochondrial calcium uniporter|Mitochondrial calcium uniporter]]
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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 6o58" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bai, X]]
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[[Category: Bai X]]
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[[Category: Jiang, Y]]
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[[Category: Jiang Y]]
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[[Category: Wang, Y]]
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[[Category: Wang Y]]
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[[Category: Complex]]
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[[Category: Ion channel]]
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[[Category: Membrane protein]]
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[[Category: Transport protein]]
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Current revision

Human MCU-EMRE complex, dimer of channel

6o58, resolution 3.80Å

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