4NXW
Crystal structure of the cytosolic domain of human MiD51
Summary for 4NXW
| Entry DOI | 10.2210/pdb4nxw/pdb |
| Related | 4NXT 4NXU 4NXV 4NXX |
| Descriptor | Mitochondrial dynamic protein MID51, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | protein-nucleotide complex, nucleotidyltransferase, protein-protein interaction, adp, gdp, mitochondrial fission, mitochondria membrane-anchored, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion outer membrane; Single-pass membrane protein: Q9NQG6 |
| Total number of polymer chains | 1 |
| Total formula weight | 38616.17 |
| Authors | Richter, V.,Kvansakul, M.,Ryan, M.T. (deposition date: 2013-12-09, release date: 2013-12-25, Last modification date: 2024-02-28) |
| Primary citation | Richter, V.,Palmer, C.S.,Osellame, L.D.,Singh, A.P.,Elgass, K.,Stroud, D.A.,Sesaki, H.,Kvansakul, M.,Ryan, M.T. Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission. J.Cell Biol., 204:477-486, 2014 Cited by PubMed Abstract: Mitochondrial fission is important for organelle transport, inheritance, and turnover, and alterations in fission are seen in neurological disease. In mammals, mitochondrial fission is executed by dynamin-related protein 1 (Drp1), a cytosolic guanosine triphosphatase that polymerizes and constricts the organelle. Recruitment of Drp1 to mitochondria involves receptors including Mff, MiD49, and MiD51. MiD49/51 form foci at mitochondrial constriction sites and coassemble with Drp1 to drive fission. Here, we solved the crystal structure of the cytosolic domain of human MiD51, which adopts a nucleotidyltransferase fold. Although MiD51 lacks catalytic residues for transferase activity, it specifically binds guanosine diphosphate and adenosine diphosphate. MiD51 mutants unable to bind nucleotides were still able to recruit Drp1. Disruption of an additional region in MiD51 that is not part of the nucleotidyltransferase fold blocked Drp1 recruitment and assembly of MiD51 into foci. MiD51 foci are also dependent on the presence of Drp1, and after scission they are distributed to daughter organelles, supporting the involvement of MiD51 in the fission apparatus. PubMed: 24515348DOI: 10.1083/jcb.201311014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
Download full validation report
