6d80

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'''Unreleased structure'''
 
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The entry 6d80 is ON HOLD until Paper Publication
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==Cryo-EM structure of the mitochondrial calcium uniporter from N. fischeri bound to saposin==
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<SX load='6d80' size='340' side='right' viewer='molstar' caption='[[6d80]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6d80]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fischeri Aspergillus fischeri] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D80 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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d80 OCA], [https://pdbe.org/6d80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d80 RCSB], [https://www.ebi.ac.uk/pdbsum/6d80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d80 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A1CWT6_NEOFI A1CWT6_NEOFI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial calcium uniporter (MCU) is a highly selective calcium channel localized to the inner mitochondrial membrane. Here, we describe the structure of an MCU orthologue from the fungus Neosartorya fischeri (NfMCU) determined to 3.8 A resolution by phase-plate cryo-electron microscopy. The channel is a homotetramer with two-fold symmetry in its amino-terminal domain (NTD) that adopts a similar structure to that of human MCU. The NTD assembles as a dimer of dimers to form a tetrameric ring that connects to the transmembrane domain through an elongated coiled-coil domain. The ion-conducting pore domain maintains four-fold symmetry, with the selectivity filter positioned at the start of the pore-forming TM2 helix. The aspartate and glutamate sidechains of the conserved DIME motif are oriented towards the central axis and separated by one helical turn. The structure of NfMCU offers insights into channel assembly, selective calcium permeation, and inhibitor binding.
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Authors:
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Cryo-EM structure of a fungal mitochondrial calcium uniporter.,Nguyen NX, Armache JP, Lee C, Yang Y, Zeng W, Mootha VK, Cheng Y, Bai XC, Jiang Y Nature. 2018 Jul 11. pii: 10.1038/s41586-018-0333-6. doi:, 10.1038/s41586-018-0333-6. PMID:29995855<ref>PMID:29995855</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6d80" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Mitochondrial calcium uniporter|Mitochondrial calcium uniporter]]
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*[[Saposin|Saposin]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Aspergillus fischeri]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Armache J-P]]
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[[Category: Bai XC]]
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[[Category: Cheng Y]]
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[[Category: Nguyen NX]]

Current revision

Cryo-EM structure of the mitochondrial calcium uniporter from N. fischeri bound to saposin

6d80, resolution 5.00Å

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