5W0T

Crystal structure of monomeric Msp1 from S. cerevisiae

5W0T の概要

• エントリーDOI: 10.2210/pdb5w0t/pdb
• 分子名称: Protein MSP1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: hydrolase, aaa atpase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34653.46

構造登録者

Keenan, R.J.,Wohlever, M.L.,Mateja, A.M. (登録日: 2017-05-31, 公開日: 2017-08-02, 最終更新日: 2024-10-16)

主引用文献

Wohlever, M.L.,Mateja, A.,McGilvray, P.T.,Day, K.J.,Keenan, R.J.
Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.
Mol. Cell, 67:194-202.e6, 2017

PubMed Abstract: Mislocalized tail-anchored (TA) proteins of the outer mitochondrial membrane are cleared by a newly identified quality control pathway involving the conserved eukaryotic protein Msp1 (ATAD1 in humans). Msp1 is a transmembrane AAA-ATPase, but its role in TA protein clearance is not known. Here, using purified components reconstituted into proteoliposomes, we show that Msp1 is both necessary and sufficient to drive the ATP-dependent extraction of TA proteins from the membrane. A crystal structure of the Msp1 cytosolic region modeled into a ring hexamer suggests that active Msp1 contains a conserved membrane-facing surface adjacent to a central pore. Structure-guided mutagenesis of the pore residues shows that they are critical for TA protein extraction in vitro and for functional complementation of an msp1 deletion in yeast. Together, these data provide a molecular framework for Msp1-dependent extraction of mislocalized TA proteins from the outer mitochondrial membrane.

PubMed: 28712723
DOI: 10.1016/j.molcel.2017.06.019

実験手法

X-RAY DIFFRACTION (2.63 Å)