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TitleStructure of the mitochondrial import gate reveals distinct preprotein paths.
Journal, issue, pagesNature, Vol. 575, Issue 7782, Page 395-401, Year 2019
Publish dateOct 10, 2019
AuthorsYuhei Araiso / Akihisa Tsutsumi / Jian Qiu / Kenichiro Imai / Takuya Shiota / Jiyao Song / Caroline Lindau / Lena-Sophie Wenz / Haruka Sakaue / Kaori Yunoki / Shin Kawano / Junko Suzuki / Marilena Wischnewski / Conny Schütze / Hirotaka Ariyama / Toshio Ando / Thomas Becker / Trevor Lithgow / Nils Wiedemann / Nikolaus Pfanner / Masahide Kikkawa / Toshiya Endo /
PubMed AbstractThe translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex at 3.8-Å ...The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex 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. Each Tom40 β-barrel is surrounded by small TOM subunits, and tethered by two Tom22 subunits and one phospholipid. The N-terminal extension of Tom40 forms a helix inside the channel; mutational analysis reveals its dual role in early and late steps in the biogenesis of intermembrane-space proteins in cooperation with Tom5. Each Tom40 channel possesses two precursor exit sites. Tom22, Tom40 and Tom7 guide presequence-containing preproteins to the exit in the middle of the dimer, whereas Tom5 and the Tom40 N extension guide preproteins lacking a presequence to the exit at the periphery of the dimer.
External linksNature / PubMed:31600774
MethodsEM (single particle)
Resolution3.81 Å
Structure data

9851

6jnf

EMDB-9851: membrane structure
PDB-6jnf: Cryo-EM structure of the translocator of the outer mitochondrial membrane
Method: EM (single particle) / Resolution: 3.81 Å

Chemicals

ChemComp-46E:
(2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl tetradecanoate

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsTRANSLOCASE / alpha/beta translocator / membrane protein complex / Protein import / mitochondria

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