6d80: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6d80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d80 OCA], [http://pdbe.org/6d80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d80 RCSB], [http://www.ebi.ac.uk/pdbsum/6d80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d80 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6d80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d80 OCA], [http://pdbe.org/6d80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d80 RCSB], [http://www.ebi.ac.uk/pdbsum/6d80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d80 ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6d80" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:36, 25 July 2018
Cryo-EM structure of the mitochondrial calcium uniporter from N. fischeri bound to saposinCryo-EM structure of the mitochondrial calcium uniporter from N. fischeri bound to saposin
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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