8u0x

Yeast Pex6 N1(1-184) DomainYeast Pex6 N1(1-184) Domain

Structural highlights

8u0x is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.86Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PEX6_YEAST Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:15634331, PubMed:16007078, PubMed:16911527, PubMed:26170309, PubMed:26066397, PubMed:29321502). Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (PubMed:26170309, PubMed:26066397, PubMed:29321502). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (PubMed:29321502).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Birschmann I, Rosenkranz K, Erdmann R, Kunau WH. Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p. FEBS J. 2005 Jan;272(1):47-58. PMID:15634331 doi:10.1111/j.1432-1033.2004.04393.x
↑ Platta HW, Grunau S, Rosenkranz K, Girzalsky W, Erdmann R. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol. 2005 Aug;7(8):817-22. PMID:16007078 doi:10.1038/ncb1281
↑ Rosenkranz K, Birschmann I, Grunau S, Girzalsky W, Kunau WH, Erdmann R. Functional association of the AAA complex and the peroxisomal importomer. FEBS J. 2006 Aug;273(16):3804-15. PMID:16911527 doi:10.1111/j.1742-4658.2006.05388.x
↑ Ciniawsky S, Grimm I, Saffian D, Girzalsky W, Erdmann R, Wendler P. Molecular snapshots of the Pex1/6 AAA+ complex in action. Nat Commun. 2015 Jun 12;6:7331. PMID:26066397 doi:10.1038/ncomms8331
↑ Blok NB, Tan D, Wang RY, Penczek PA, Baker D, DiMaio F, Rapoport TA, Walz T. Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy. Proc Natl Acad Sci U S A. 2015 Jul 28;112(30):E4017-25. PMID:26170309 doi:10.1073/pnas.1500257112
↑ Gardner BM, Castanzo DT, Chowdhury S, Stjepanovic G, Stefely MS, Hurley JH, Lander GC, Martin A. The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. Nat Commun. 2018 Jan 10;9(1):135. doi: 10.1038/s41467-017-02474-4. PMID:29321502 doi:http://dx.doi.org/10.1038/s41467-017-02474-4

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OCA

[1] Birschmann I, Rosenkranz K, Erdmann R, Kunau WH. Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p. FEBS J. 2005 Jan;272(1):47-58. PMID:15634331 doi:10.1111/j.1432-1033.2004.04393.x

[2] Platta HW, Grunau S, Rosenkranz K, Girzalsky W, Erdmann R. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol. 2005 Aug;7(8):817-22. PMID:16007078 doi:10.1038/ncb1281

[3] Rosenkranz K, Birschmann I, Grunau S, Girzalsky W, Kunau WH, Erdmann R. Functional association of the AAA complex and the peroxisomal importomer. FEBS J. 2006 Aug;273(16):3804-15. PMID:16911527 doi:10.1111/j.1742-4658.2006.05388.x

[4] Ciniawsky S, Grimm I, Saffian D, Girzalsky W, Erdmann R, Wendler P. Molecular snapshots of the Pex1/6 AAA+ complex in action. Nat Commun. 2015 Jun 12;6:7331. PMID:26066397 doi:10.1038/ncomms8331

[5] Blok NB, Tan D, Wang RY, Penczek PA, Baker D, DiMaio F, Rapoport TA, Walz T. Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy. Proc Natl Acad Sci U S A. 2015 Jul 28;112(30):E4017-25. PMID:26170309 doi:10.1073/pnas.1500257112

[6] Gardner BM, Castanzo DT, Chowdhury S, Stjepanovic G, Stefely MS, Hurley JH, Lander GC, Martin A. The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. Nat Commun. 2018 Jan 10;9(1):135. doi: 10.1038/s41467-017-02474-4. PMID:29321502 doi:http://dx.doi.org/10.1038/s41467-017-02474-4

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