5VXV
Peroxisomal membrane protein PEX15
5VXV の概要
エントリーDOI | 10.2210/pdb5vxv/pdb |
分子名称 | Peroxisomal membrane protein PEX15 (2 entities in total) |
機能のキーワード | alpha helical, membrane protein |
由来する生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 25567.15 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 29321502DOI: 10.1038/s41467-017-02474-4 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.55 Å) |
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