Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism.

ABSTRACT: The mitochondrial uniporter is a Ca²⁺-channel complex resident within the organelle's inner membrane. In mammalian cells the uniporter's activity is regulated by Ca²⁺ due to concerted action of MICU1 and MICU2, two paralogous, but functionally distinct, EF-hand Ca²⁺-binding proteins. Here we present the X-ray structure of the apo form of Mus musculus MICU2 at 2.5-Å resolution. The core structure of MICU2 is very similar to that of MICU1. It consists of two lobes, each containing one canonical Ca²⁺-binding EF-hand (EF1, EF4) and one structural EF-hand (EF2, EF3). Two molecules of MICU2 form a symmetrical dimer stabilized by highly conserved hydrophobic contacts between exposed residues of EF1 of one monomer and EF3 of another. Similar inter

SUBMITTER: Kamer KJ 

PROVIDER: S-EPMC6397551 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature