Cryo-EM structure of the translocator of the outer mitochondrial membrane
Ontology highlight
ABSTRACT:
SUBMITTER: Toshiya Endo
PROVIDER: EMPIAR-10332 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure of the mitochondrial import gate reveals distinct preprotein paths.
Araiso Yuhei Y Tsutsumi Akihisa A Qiu Jian J Imai Kenichiro K Shiota Takuya T Song Jiyao J Lindau Caroline C Wenz Lena-Sophie LS Sakaue Haruka H Yunoki Kaori K Kawano Shin S Suzuki Junko J Wischnewski Marilena M Schütze Conny C Ariyama Hirotaka H Ando Toshio T Becker Thomas T Lithgow Trevor T Wiedemann Nils N Pfanner Nikolaus N Kikkawa Masahide M Endo Toshiya T
Nature 20191010 7782
The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins<sup>1-4</sup>. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex<sup>5-9</sup> at 3.8-Å resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 β-barrel channels and α-helical transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes<sup>1-3</sup>. Each Tom40 β-barr ...[more]
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