Department of Biochemistry, School of Medicine, University of Utah, Salt Lake City, UT, USA.
Nat Struct Mol Biol. 2020 Mar;27(3):225-226. doi: 10.1038/s41594-020-0389-5.
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 now reveal that Bcs1 adopts an unusual heptameric configuration and provide insights into a non-canonical translocation mechanism.
许多 AAA+ ATP 酶组装成六聚体,使用手对手、穿线机制展开蛋白质底物,但 Bcs1 AAA+ ATP 酶促进折叠的、含铁硫 Rieske 蛋白的线粒体膜易位。现在有两份报告揭示了 Bcs1 采用了一种不寻常的七聚体构象,并提供了对非典型易位机制的深入了解。