Movie
Controller
Structure viewers
About EMN Papers
+Search query
-Structure paper
| Title | The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 135, Year 2018 |
| Publish date | Jan 10, 2018 |
 Authors | Brooke M Gardner / Dominic T Castanzo / Saikat Chowdhury / Goran Stjepanovic / Matthew S Stefely / James H Hurley / Gabriel C Lander / Andreas Martin /  |
| 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 ...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. |
 External links | Nat Commun / PubMed:29321502 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 1.55 - 23.2 Å |
| Structure data |  EMDB-7005:  PDB-5vxv: |
| Chemicals |  ChemComp-HOH: |
| Source |
|
 Keywords |  MEMBRANE PROTEIN / alpha helical |
