6dnf: 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=6dnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnf OCA], [http://pdbe.org/6dnf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dnf RCSB], [http://www.ebi.ac.uk/pdbsum/6dnf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnf 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=6dnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnf OCA], [http://pdbe.org/6dnf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dnf RCSB], [http://www.ebi.ac.uk/pdbsum/6dnf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnf ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The mitochondrial calcium uniporter (MCU) is a highly selective calcium channel and a major route of calcium entry into mitochondria. How the channel catalyses ion permeation and achieves ion selectivity are not well understood, partly because MCU is thought to have a distinct architecture in comparison to other cellular channels. Here we report cryo-electron microscopy reconstructions of MCU channels from zebrafish and Cyphellophora europaea at 8.5 A and 3.2 A resolutions, respectively. In contrast to a previous report of pentameric stoichiometry for MCU, both channels are tetramers. The atomic model of C. europaea MCU shows that a conserved WDXXEP signature sequence forms the selectivity filter, in which calcium ions are arranged in single file. Coiled-coil legs connect the pore to N-terminal domains in the mitochondrial matrix. In C. europaea MCU, the N-terminal domains assemble as a dimer of dimers; in zebrafish MCU, they form an asymmetric crescent. The structures define principles that underlie ion permeation and calcium selectivity in this unusual channel. | |||
Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters.,Baradaran R, Wang C, Siliciano AF, Long SB Nature. 2018 Jul 11. pii: 10.1038/s41586-018-0331-8. doi:, 10.1038/s41586-018-0331-8. PMID:29995857<ref>PMID:29995857</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6dnf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 10:38, 25 July 2018
Cryo-EM structure of the mitochondrial calcium uniporter MCU from the fungus Cyphellophora europaeaCryo-EM structure of the mitochondrial calcium uniporter MCU from the fungus Cyphellophora europaea
Structural highlights
Publication Abstract from PubMedThe mitochondrial calcium uniporter (MCU) is a highly selective calcium channel and a major route of calcium entry into mitochondria. How the channel catalyses ion permeation and achieves ion selectivity are not well understood, partly because MCU is thought to have a distinct architecture in comparison to other cellular channels. Here we report cryo-electron microscopy reconstructions of MCU channels from zebrafish and Cyphellophora europaea at 8.5 A and 3.2 A resolutions, respectively. In contrast to a previous report of pentameric stoichiometry for MCU, both channels are tetramers. The atomic model of C. europaea MCU shows that a conserved WDXXEP signature sequence forms the selectivity filter, in which calcium ions are arranged in single file. Coiled-coil legs connect the pore to N-terminal domains in the mitochondrial matrix. In C. europaea MCU, the N-terminal domains assemble as a dimer of dimers; in zebrafish MCU, they form an asymmetric crescent. The structures define principles that underlie ion permeation and calcium selectivity in this unusual channel. Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters.,Baradaran R, Wang C, Siliciano AF, Long SB Nature. 2018 Jul 11. pii: 10.1038/s41586-018-0331-8. doi:, 10.1038/s41586-018-0331-8. PMID:29995857[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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