6D80

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

Summary for 6D80

• Entry DOI: 10.2210/pdb6d80/pdb
• Related: 6D7W
• EMDB information: 7826 7828
• Descriptor: Saposin A, Mitochondrial calcium uniporter, CALCIUM ION (3 entities in total)
• Functional Keywords: mitochondria, calcium channel, transport protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 10
• Total formula weight: 233221.16

Authors

Nguyen, N.X.,Armache, J.-P.,Cheng, Y.,Bai, X.C. (deposition date: 2018-04-25, release date: 2018-07-11, Last modification date: 2025-05-21)

Primary citation

Nguyen, N.X.,Armache, J.-P.,Lee, C.,Yang, Y.,Zeng, W.,Mootha, V.K.,Cheng, Y.,Bai, X.C.,Jiang, Y.
Cryo-EM structure of a fungal mitochondrial calcium uniporter.
Nature, 559:570-574, 2018

PubMed Abstract: 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 Å 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.

PubMed: 29995855
DOI: 10.1038/s41586-018-0333-6

Experimental method

ELECTRON MICROSCOPY (5 Å)