Many AAA+ ATPases assemble as hexamers to unfold protein substrates using a hand-over-hand, threading mechanism, but the Bcs1 AAA+ ATPase facilitates mitochondrial membrane translocation of the folded iron–sulfur Rieske protein. Two reports reveal that Bcs1 adopts an unusual heptameric configuration and provide insights into a non-canonical translocation mechanism.

中文翻译：

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重新排列 AAA+ 架构以适应折叠基板。

许多 AAA+ ATP 酶组装成六聚体，使用手递、穿线机制展开蛋白质底物，但 Bcs1 AAA+ ATP 酶促进折叠的铁-硫 Rieske 蛋白的线粒体膜易位。两份报告显示 Bcs1 采用了一种不寻常的七聚体配置，并提供了对非规范易位机制的见解。