5z2i

Structure of Dictyostelium discoideum mitochondrial calcium uniporter N-ternimal domain (Se-DdMCU-NTD)

spinqualitylabelsall models 5z2i, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5z2i is a 4 chain structure with sequence from Dicdi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: DDB0186972 (DICDI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MCU_DICDI] Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:24889638). Constitutes a pore-forming and calcium-conducting subunit (PubMed:24889638). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.[UniProtKB:Q8NE86] Publication Abstract from PubMed The mitochondrial calcium uniporter (MCU) plays a critical role in mitochondrial calcium uptake into the matrix. In metazoans, the uniporter is a tightly regulated multicomponent system, including the pore-forming subunit MCU and several regulators (MICU1, MICU2, and Essential MCU REgulator, EMRE). The calcium-conducting activity of metazoan MCU requires the single-transmembrane protein EMRE. Dictyostelium discoideum (Dd), however, developed a simplified uniporter for which the pore-forming MCU (DdMCU) alone is necessary and sufficient for calcium influx. Here, we report a crystal structure of the N-terminal domain (NTD) of DdMCU at 1.7 A resolution. The DdMCU-NTD contains four helices and two strands arranged in a fold that is completely different from the known structures of other MCU-NTD homologues. Biochemical and biophysical analyses of DdMCU-NTD in solution indicated that the domain exists as high-order oligomers. Mutagenesis showed that the acidic residues Asp60, Glu72, and Glu74, which appeared to mediate the interface II, as observed in the crystal structure, participated in the self-assembly of DdMCU-NTD. Intriguingly, the oligomeric complex was disrupted in the presence of calcium. We propose that the calcium-triggered dissociation of NTD regulates the channel activity of DdMCU by a yet unknown mechanism. Structural Characterization of the N-Terminal Domain of the Dictyostelium discoideum Mitochondrial Calcium Uniporter.,Yuan Y, Cao C, Wen M, Li M, Dong Y, Wu L, Wu J, Cui T, Li D, Chou JJ, OuYang B ACS Omega. 2020 Mar 20;5(12):6452-6460. doi: 10.1021/acsomega.9b04045., eCollection 2020 Mar 31. PMID:32258880 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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