Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold for Sam35 and Sam37 and sheds light on how the S...

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Auteurs principaux:	Kathryn A. Diederichs, Xiaodan Ni, Sarah E. Rollauer, Istvan Botos, Xiaofeng Tan, Martin S. King, Edmund R. S. Kunji, Jiansen Jiang, Susan K. Buchanan
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2020
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/17cd9cca86824dddb42a0249449c47c3
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id	oai:doaj.org-article:17cd9cca86824dddb42a0249449c47c3
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spelling	oai:doaj.org-article:17cd9cca86824dddb42a0249449c47c32021-12-02T14:34:13ZStructural insight into mitochondrial β-barrel outer membrane protein biogenesis10.1038/s41467-020-17144-12041-1723https://doaj.org/article/17cd9cca86824dddb42a0249449c47c32020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17144-1https://doaj.org/toc/2041-1723The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold for Sam35 and Sam37 and sheds light on how the Sam50 beta-barrel opens a lateral gate to accommodate its substrates.Kathryn A. DiederichsXiaodan NiSarah E. RollauerIstvan BotosXiaofeng TanMartin S. KingEdmund R. S. KunjiJiansen JiangSusan K. BuchananNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kathryn A. Diederichs Xiaodan Ni Sarah E. Rollauer Istvan Botos Xiaofeng Tan Martin S. King Edmund R. S. Kunji Jiansen Jiang Susan K. Buchanan Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
description	The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold for Sam35 and Sam37 and sheds light on how the Sam50 beta-barrel opens a lateral gate to accommodate its substrates.
format	article
author	Kathryn A. Diederichs Xiaodan Ni Sarah E. Rollauer Istvan Botos Xiaofeng Tan Martin S. King Edmund R. S. Kunji Jiansen Jiang Susan K. Buchanan
author_facet	Kathryn A. Diederichs Xiaodan Ni Sarah E. Rollauer Istvan Botos Xiaofeng Tan Martin S. King Edmund R. S. Kunji Jiansen Jiang Susan K. Buchanan
author_sort	Kathryn A. Diederichs
title	Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_short	Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_full	Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_fullStr	Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_full_unstemmed	Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_sort	structural insight into mitochondrial β-barrel outer membrane protein biogenesis
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/17cd9cca86824dddb42a0249449c47c3
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Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

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