7pv1
From Proteopedia
Crystal structure of the dimeric mitofilin domain of Mic60 in complex with the CHCH domain of Mic19
Structural highlights
FunctionG0S140_CHATD G0SHY5_CHATD Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway.[ARBA:ARBA00025571] Publication Abstract from PubMedMitochondrial 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. Structural insights into crista junction formation by the Mic60-Mic19 complex.,Bock-Bierbaum T, Funck K, Wollweber F, Lisicki E, von der Malsburg K, von der Malsburg A, Laborenz J, Noel JK, Hessenberger M, Jungbluth S, Bernert C, Kunz S, Riedel D, Lilie H, Jakobs S, van der Laan M, Daumke O Sci Adv. 2022 Sep 2;8(35):eabo4946. doi: 10.1126/sciadv.abo4946. Epub 2022 Aug, 31. PMID:36044574[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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