5x9b | pdb_00005x9b

Crystal structure of the cytosolic domain of human MiD51

spinqualitylabelsall models 5x9b, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x9b is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5x9c Gene: MID51 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MID51_HUMAN] Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Publication Abstract from PubMed Mitochondrial fission is facilitated by dynamin-related protein Drp1 and a variety of its receptors. However, the molecular mechanism of how Drp1 is recruited to the mitochondrial surface by receptors MiD49 and MiD51 remains elusive. Here, we showed that the interaction between Drp1 and MiD51 is regulated by GTP binding and depends on the polymerization of Drp1. We identified two regions on MiD51 that directly bind to Drp1, and found that dimerization of MiD51, relevant to residue C452, is required for mitochondrial dynamics regulation. Our Results have suggested a multi-faceted regulatory mechanism for the interaction between Drp1 and MiD51 that illustrates the potentially complicated and tight regulation of mitochondrial fission. New interfaces on MiD51 for Drp1 recruitment and regulation.,Ma J, Zhai Y, Chen M, Zhang K, Chen Q, Pang X, Sun F PLoS One. 2019 Jan 31;14(1):e0211459. doi: 10.1371/journal.pone.0211459., eCollection 2019. PMID:30703167 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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