Molecular snapshots of the Pex1/6 AAA+ complex in action

Susanne Ciniawsky, Immanuel Grimm, Delia Saffian, Wolfgang Girzalsky, Ralf Erdmann and Petra Wendler ()
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Susanne Ciniawsky: Gene Center Munich, Ludwig-Maximilians-Universität München
Immanuel Grimm: Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum
Delia Saffian: Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum
Wolfgang Girzalsky: Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum
Ralf Erdmann: Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum
Petra Wendler: Gene Center Munich, Ludwig-Maximilians-Universität München

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract 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.

Date: 2015
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DOI: 10.1038/ncomms8331

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