6AGH
Crystal structure of EFHA1 in Apo-State
Summary for 6AGH
| Entry DOI | 10.2210/pdb6agh/pdb |
| Descriptor | Calcium uptake protein 2, mitochondrial (2 entities in total) |
| Functional Keywords | mitochondrial, calcium, calcium binding protein, metal binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 79484.92 |
| Authors | Yangfei, X.,Xue, Y.,Yuequan, S. (deposition date: 2018-08-11, release date: 2019-01-23, Last modification date: 2023-11-22) |
| Primary citation | Xing, Y.,Wang, M.,Wang, J.,Nie, Z.,Wu, G.,Yang, X.,Shen, Y. Dimerization of MICU Proteins Controls Ca2+Influx through the Mitochondrial Ca2+Uniporter. Cell Rep, 26:1203-1212.e4, 2019 Cited by PubMed Abstract: The mitochondrial Ca uniporter complex (MCUC) is responsible for Ca influx into the mitochondrial matrix, playing critical roles in various mitochondrial functions. Eukaryotic MCUC consists of multiple subunits, and its Ca influx activity is controlled by regulatory subunits, including mitochondrial Ca uptake 1 (MICU1) and its paralogs (MICU2 and MICU3). However, the underlying mechanism remains unclear. Here, we determined multiple crystal structures of MICU2 and MICU3 from Homo sapiens. Our data demonstrate that distinct MICU protein N-domains determine the specific type of MICU dimers that perform the opposing roles in mitochondrial Ca uptake at low cytosolic Ca levels. In contrast, at high cytosolic Ca levels, all MICU proteins undergo dimer rearrangement induced by Ca binding, which releases the suppression of the MCUC pore-forming subunit and promotes the influx of large amounts of Ca. Altogether, our results elucidate the delicate mechanism of mitochondrial Ca uptake regulation by MICU proteins. PubMed: 30699349DOI: 10.1016/j.celrep.2019.01.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.742 Å) |
Structure validation
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