7PUZ

Crystal structure of the Mic60 coiled coil domain

Summary for 7PUZ

• Entry DOI: 10.2210/pdb7puz/pdb
• Descriptor: MICOS complex subunit MIC60 (1 entity in total)
• Functional Keywords: micos, coiled coil, mitochondria, structural protein
• Biological source: Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284) (Yeast, Kluyveromyces thermotolerans)
• Total number of polymer chains: 1
• Total formula weight: 20023.63

Authors

Bock-Bierbaum, T.,Funck, K.,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

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: 36044574
DOI: 10.1126/sciadv.abo4946

Experimental method

X-RAY DIFFRACTION (2.842 Å)