|Title||Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.|
|Journal, issue, pages||Elife, Vol. 9, Year 2020|
|Publish date||Jan 30, 2020|
|Authors||Lan Wang / Alexander Myasnikov / Xingjie Pan / Peter Walter /|
|PubMed Abstract||The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization. How Msp1 selects its substrates and firmly ...The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization. How Msp1 selects its substrates and firmly engages them during the energetically unfavorable extraction process remains a mystery. To address this question, we solved cryo-EM structures of Msp1-substrate complexes at near-atomic resolution. Akin to other AAA proteins, Msp1 forms hexameric spirals that translocate substrates through a central pore. A singular hydrophobic substrate recruitment site is exposed at the spiral's seam, which we propose positions the substrate for entry into the pore. There, a tight web of aromatic amino acids grips the substrate in a sequence-promiscuous, hydrophobic milieu. Elements at the intersubunit interfaces coordinate ATP hydrolysis with the subunits' positions in the spiral. We present a comprehensive model of Msp1's mechanism, which follows general architectural principles established for other AAA proteins yet specializes Msp1 for its unique role in membrane protein extraction.|
|External links||PubMed:31999255 / Publisher's page|
|Keywords||PROTEIN TRANSPORT / membrane protein / tail-anchored protein / protein quality control|
|Methods||EM (single particle)|
|Resolution||3.1 - 3.7 A|
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