| http://purl.uniprot.org/citations/25581164 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25581164 | http://www.w3.org/2000/01/rdf-schema#comment | "Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface, where assembly leads to activation of its GTP-dependent scission function. MiD49 and MiD51 are two receptors on the mitochondrial outer membrane that can recruit Drp1 to facilitate mitochondrial fission. Structural studies indicated that MiD51 has a variant nucleotidyl transferase fold that binds an ADP co-factor essential for activation of Drp1 function. MiD49 shares sequence homology with MiD51 and regulates Drp1 function. However, it is unknown if MiD49 binds an analogous co-factor. Because MiD49 does not readily crystallize, we used structural predictions and biochemical screening to identify a surface entropy reduction mutant that facilitated crystallization. Using molecular replacement, we determined the atomic structure of MiD49 to 2.4 Å. Like MiD51, MiD49 contains a nucleotidyl transferase domain; however, the electron density provides no evidence for a small-molecule ligand. Structural changes in the putative nucleotide-binding pocket make MiD49 incompatible with an extended ligand like ADP, and critical nucleotide-binding residues found in MiD51 are not conserved. MiD49 contains a surface loop that physically interacts with Drp1 and is necessary for Drp1 recruitment to the mitochondrial surface. Our results suggest a structural basis for the differential regulation of MiD51- versus MiD49-mediated fission."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.org/dc/terms/identifier | "doi:10.1002/pro.2629"xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Liu R."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Meng S."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Kaiser J.T."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Chan D.C."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Loson O.C."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/author | "Ngo H."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/name | "Protein Sci"xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/pages | "386-394"xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/title | "Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1."xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://purl.uniprot.org/core/volume | "24"xsd:string |
| http://purl.uniprot.org/citations/25581164 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25581164 |
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