5VXV

Peroxisomal membrane protein PEX15

Summary for 5VXV

• Entry DOI: 10.2210/pdb5vxv/pdb
• Descriptor: Peroxisomal membrane protein PEX15 (2 entities in total)
• Functional Keywords: alpha helical, membrane protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 25567.15

Authors

Gardner, B.M.,Castanzo, D.T. (deposition date: 2017-05-24, release date: 2018-01-17, Last modification date: 2024-11-20)

Primary citation

Gardner, B.M.,Castanzo, D.T.,Chowdhury, S.,Stjepanovic, G.,Stefely, M.S.,Hurley, J.H.,Lander, G.C.,Martin, A.
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.
Nat Commun, 9:135-135, 2018

PubMed Abstract: Pex1 and Pex6 form a heterohexameric motor essential for peroxisome biogenesis and function, and mutations in these AAA-ATPases cause most peroxisome-biogenesis disorders in humans. The tail-anchored protein Pex15 recruits Pex1/Pex6 to the peroxisomal membrane, where it performs an unknown function required for matrix-protein import. Here we determine that Pex1/Pex6 from S. cerevisiae is a protein translocase that unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Our structural studies of Pex15 in isolation and in complex with Pex1/Pex6 illustrate that Pex15 binds the N-terminal domains of Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery. Our results thus support a role of Pex1/Pex6 in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import.

PubMed: 29321502
DOI: 10.1038/s41467-017-02474-4

Experimental method

X-RAY DIFFRACTION (1.55 Å)