6LE5
Crystal structure of the mitochondrial calcium uptake 1 and 2 heterodimer (MICU1-MICU2 heterodimer) in an apo state
Summary for 6LE5
| Entry DOI | 10.2210/pdb6le5/pdb |
| Descriptor | Calcium uptake protein 1, mitochondrial, Calcium uptake protein 2, mitochondrial (2 entities in total) |
| Functional Keywords | complex, mitochondrial calcium uptake 1 and mitochondrial calcium uptake 2, metal binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 318078.26 |
| Authors | |
| Primary citation | Park, J.,Lee, Y.,Park, T.,Kang, J.Y.,Mun, S.A.,Jin, M.,Yang, J.,Eom, S.H. Structure of the MICU1-MICU2 heterodimer provides insights into the gatekeeping threshold shift. Iucrj, 7:355-365, 2020 Cited by PubMed Abstract: Mitochondrial calcium uptake proteins 1 and 2 (MICU1 and MICU2) mediate mitochondrial Ca influx via the mitochondrial calcium uniporter (MCU). Its molecular action for Ca uptake is tightly controlled by the MICU1-MICU2 heterodimer, which comprises Ca sensing proteins which act as gatekeepers at low [Ca] or facilitators at high [Ca]. However, the mechanism underlying the regulation of the Ca gatekeeping threshold for mitochondrial Ca uptake through the MCU by the MICU1-MICU2 heterodimer remains unclear. In this study, we determined the crystal structure of the apo form of the human MICU1-MICU2 heterodimer that functions as the MCU gatekeeper. MICU1 and MICU2 assemble in the face-to-face heterodimer with salt bridges and me-thio-nine knobs stabilizing the heterodimer in an apo state. Structural analysis suggests how the heterodimer sets a higher Ca threshold than the MICU1 homodimer. The structure of the heterodimer in the apo state provides a framework for understanding the gatekeeping role of the MICU1-MICU2 heterodimer. PubMed: 32148862DOI: 10.1107/S2052252520001840 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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