7PV0
Crystal structure of a Mic60-Mic19 fusion protein
Summary for 7PV0
| Entry DOI | 10.2210/pdb7pv0/pdb |
| Related | 7PUZ 7PV1 |
| Descriptor | MICOS complex subunit MIC60,MICOS complex subunit MIC60-MIC19,Mic60-Mic19, O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500) (3 entities in total) |
| Functional Keywords | micos, mitofilin, chch, mitochondria, structural protein |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) More |
| Total number of polymer chains | 6 |
| Total formula weight | 62823.02 |
| Authors | Funck, K.,Bock-Bierbaum, T.,Daumke, O. (deposition date: 2021-10-01, release date: 2022-09-07, Last modification date: 2024-05-01) |
| Primary citation | Bock-Bierbaum, T.,Funck, K.,Wollweber, F.,Lisicki, E.,von der Malsburg, K.,von der Malsburg, A.,Laborenz, J.,Noel, J.K.,Hessenberger, M.,Jungbluth, S.,Bernert, C.,Kunz, S.,Riedel, D.,Lilie, H.,Jakobs, S.,van der Laan, M.,Daumke, O. Structural insights into crista junction formation by the Mic60-Mic19 complex. Sci Adv, 8:eabo4946-eabo4946, 2022 Cited by PubMed Abstract: Mitochondrial cristae membranes are the oxidative phosphorylation sites in cells. Crista junctions (CJs) form the highly curved neck regions of cristae and are thought to function as selective entry gates into the cristae space. Little is known about how CJs are generated and maintained. We show that the central coiled-coil (CC) domain of the mitochondrial contact site and cristae organizing system subunit Mic60 forms an elongated, bow tie-shaped tetrameric assembly. Mic19 promotes Mic60 tetramerization via a conserved interface between the Mic60 mitofilin and Mic19 CHCH (CC-helix-CC-helix) domains. Dimerization of mitofilin domains exposes a crescent-shaped membrane-binding site with convex curvature tailored to interact with the curved CJ neck. Our study suggests that the Mic60-Mic19 subcomplex traverses CJs as a molecular strut, thereby controlling CJ architecture and function. PubMed: 36044574DOI: 10.1126/sciadv.abo4946 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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