6XQO
Structure of the human MICU1-MICU2 heterodimer, calcium bound, in association with a lipid nanodisc
Summary for 6XQO
| Entry DOI | 10.2210/pdb6xqo/pdb |
| EMDB information | 22290 22291 |
| Descriptor | Calcium uptake protein 1, mitochondrial, Calcium uptake protein 2, mitochondrial, CALCIUM ION (3 entities in total) |
| Functional Keywords | ion channel, calcium channel, mitochondrial calcium uniporter, mcu, emre, mitochondria, calcium binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 90563.80 |
| Authors | Long, S.B.,Wang, C.,Baradaran, R.,Jacewicz, A.,Delgado, B. (deposition date: 2020-07-09, release date: 2020-07-29, Last modification date: 2024-03-06) |
| Primary citation | Wang, C.,Jacewicz, A.,Delgado, B.D.,Baradaran, R.,Long, S.B. Structures reveal gatekeeping of the mitochondrial Ca 2+ uniporter by MICU1-MICU2. Elife, 9:-, 2020 Cited by PubMed Abstract: The mitochondrial calcium uniporter is a Ca-gated ion channel complex that controls mitochondrial Ca entry and regulates cell metabolism. MCU and EMRE form the channel while Ca-dependent regulation is conferred by MICU1 and MICU2 through an enigmatic process. We present a cryo-EM structure of an MCU-EMRE-MICU1-MICU2 holocomplex comprising MCU and EMRE subunits from the beetle Tribolium castaneum in complex with a human MICU1-MICU2 heterodimer at 3.3 Å resolution. With analogy to how neuronal channels are blocked by protein toxins, a uniporter interaction domain on MICU1 binds to a channel receptor site comprising MCU and EMRE subunits to inhibit ion flow under resting Ca conditions. A Ca-bound structure of MICU1-MICU2 at 3.1 Å resolution indicates how Ca-dependent changes enable dynamic response to cytosolic Ca signals. PubMed: 32667285DOI: 10.7554/eLife.59991 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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