A multipoint guidance mechanism for β-barrel folding on the SAM complex

التفاصيل البيبلوغرافية
العنوان: A multipoint guidance mechanism for β-barrel folding on the SAM complex
المؤلفون: Hironori Takeda, Jon V. Busto, Caroline Lindau, Akihisa Tsutsumi, Kentaro Tomii, Kenichiro Imai, Yu Yamamori, Takatsugu Hirokawa, Chie Motono, Iniyan Ganesan, Lena-Sophie Wenz, Thomas Becker, Masahide Kikkawa, Nikolaus Pfanner, Nils Wiedemann, Toshiya Endo
المصدر: Nature Structural & Molecular Biology. 30:176-187
بيانات النشر: Springer Science and Business Media LLC, 2023.
سنة النشر: 2023
مصطلحات موضوعية: Structural Biology, Molecular Biology
الوصف: Mitochondrial β-barrel proteins are essential for the transport of metabolites, ions and proteins. The sorting and assembly machinery (SAM) mediates their folding and membrane insertion. We report the cryo-electron microscopy structure of the yeast SAM complex carrying an early eukaryotic β-barrel folding intermediate. The lateral gate of Sam50 is wide open and pairs with the last β-strand (β-signal) of the substrate-the 19-β-stranded Tom40 precursor-to form a hybrid barrel in the membrane plane. The Tom40 barrel grows and curves, guided by an extended bridge with Sam50. Tom40's first β-segment (β1) penetrates into the nascent barrel, interacting with its inner wall. The Tom40 amino-terminal segment then displaces β1 to promote its pairing with Tom40's last β-strand to complete barrel formation with the assistance of Sam37's dynamic α-protrusion. Our study thus reveals a multipoint guidance mechanism for mitochondrial β-barrel folding.
تدمد: 1545-9985
1545-9993
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ce01e574b7c897d843d11317c2e5e5e
https://doi.org/10.1038/s41594-022-00897-2
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....8ce01e574b7c897d843d11317c2e5e5e
قاعدة البيانات: OpenAIRE