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TitleStructure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJan 30, 2020
AuthorsLan Wang / Alexander Myasnikov / Xingjie Pan / Peter Walter /
PubMed AbstractThe 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 linksPubMed:31999255 / Publisher's page
KeywordsPROTEIN TRANSPORT / membrane protein / tail-anchored protein / protein quality control
MethodsEM (single particle)
Resolution3.1 - 3.7 A
Structure data

EMDB-20318:
Msp1-substrate complex in closed conformation

EMDB-20319:
Msp1-substrate complex in open conformation

EMDB-20320:
Msp1 (E214Q)-substrate complex

PDB-6pdw:
Msp1-substrate complex in closed conformation

PDB-6pdy:
Msp1-substrate complex in open conformation

PDB-6pe0:
Msp1 (E214Q)-substrate complex

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
MAGNESIUM ION / Magnesium

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

Source
  • chaetomium thermophilum (fungus)
  • escherichia coli (E. coli)

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