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TitleMolecular snapshots of the Pex1/6 AAA+ complex in action.
Journal, issue, pagesNat Commun, Vol. 6, Page 7331, Year 2015
Publish dateJun 12, 2015
AuthorsSusanne Ciniawsky / Immanuel Grimm / Delia Saffian / Wolfgang Girzalsky / Ralf Erdmann / Petra Wendler /
PubMed AbstractThe peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex, which fuels essential protein transport across peroxisomal membranes. Mutations in either ATPase in humans ...The peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex, which fuels essential protein transport across peroxisomal membranes. Mutations in either ATPase in humans can lead to severe peroxisomal disorders and early death. We present an extensive structural and biochemical analysis of the yeast Pex1/6 complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. Mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain, giving structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies.
External linksNat Commun / PubMed:26066397 / PubMed Central
MethodsEM (single particle)
Resolution21.0 - 24.0 Å
Structure data

EMDB-2582:
S. cerevisiae Pex1/6 wild type complex bound to ADP
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-2583:
S. cerevisiae Pex1/6 wild type complex bound to gammaS ATP
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-2584:
S. cerevisiae Pex1/6 wild type complex bound to ADP-Alfx
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-2585:
S. cerevisiae Pex1/6 wild type complex bound to ATP
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-2586:
S. cerevisiae Pex1/6 single Walker B (6WB) complex bound to ATP
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-2587:
S. cerevisiae Pex1/6 single Walker B (1WB) complex bound to ATP
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-2588:
S. cerevisiae Pex1/6 double Walker B (DWB) complex bound to ATP
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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