5X9B
Crystal structure of the cytosolic domain of human MiD51
Summary for 5X9B
Entry DOI | 10.2210/pdb5x9b/pdb |
Related | 5X9C |
Descriptor | Mitochondrial dynamics protein MID51 (2 entities in total) |
Functional Keywords | receptor, mitochondrial fission, nucleotidyltransferase fold, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 37447.00 |
Authors | |
Primary citation | Ma, J.,Zhai, Y.,Chen, M.,Zhang, K.,Chen, Q.,Pang, X.,Sun, F. New interfaces on MiD51 for Drp1 recruitment and regulation. Plos One, 14:e0211459-e0211459, 2019 Cited by PubMed Abstract: 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. PubMed: 30703167DOI: 10.1371/journal.pone.0211459 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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