6O5B

Monomer of a cation channel

Summary for 6O5B

• Entry DOI: 10.2210/pdb6o5b/pdb
• EMDB information: 0625 0626 0627
• Descriptor: Calcium uniporter protein, mitochondrial, Essential MCU regulator, mitochondrial, CALCIUM ION (3 entities in total)
• Functional Keywords: ion channel, complex, membrane protein, transport protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 365223.26

Authors

Wang, Y.,Bai, X.,Jiang, Y. (deposition date: 2019-03-01, release date: 2019-05-22, Last modification date: 2024-03-20)

Primary citation

Wang, Y.,Nguyen, N.X.,She, J.,Zeng, W.,Yang, Y.,Bai, X.C.,Jiang, Y.
Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter.
Cell, 177:1252-, 2019

PubMed Abstract: Mitochondrial calcium uptake is crucial to the regulation of eukaryotic Ca homeostasis and is mediated by the mitochondrial calcium uniporter (MCU). While MCU alone can transport Ca 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.

PubMed: 31080062
DOI: 10.1016/j.cell.2019.03.050

Experimental method

ELECTRON MICROSCOPY (3.6 Å)