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| | <StructureSection load='5vxv' size='340' side='right'caption='[[5vxv]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='5vxv' size='340' side='right'caption='[[5vxv]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vxv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VXV FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PEX15, PAS21, YOL044W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vxv OCA], [http://pdbe.org/5vxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vxv RCSB], [http://www.ebi.ac.uk/pdbsum/5vxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vxv ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vxv OCA], [https://pdbe.org/5vxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vxv RCSB], [https://www.ebi.ac.uk/pdbsum/5vxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vxv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEX15_YEAST PEX15_YEAST]] Essential for the biogenesis of peroxisomes. Has a role in anchoring PEX6 onto the peroxisomal membrane.<ref>PMID:12808025</ref> <ref>PMID:9405362</ref> | + | [https://www.uniprot.org/uniprot/PEX15_YEAST PEX15_YEAST] Essential for the biogenesis of peroxisomes. Has a role in anchoring PEX6 onto the peroxisomal membrane.<ref>PMID:12808025</ref> <ref>PMID:9405362</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Castanzo, D T]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gardner, B M]] | + | [[Category: Castanzo DT]] |
| - | [[Category: Alpha helical]] | + | [[Category: Gardner BM]] |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
PEX15_YEAST Essential for the biogenesis of peroxisomes. Has a role in anchoring PEX6 onto the peroxisomal membrane.[1] [2]
Publication Abstract from PubMed
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.
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.,Gardner BM, Castanzo DT, Chowdhury S, Stjepanovic G, Stefely MS, Hurley JH, Lander GC, Martin A Nat Commun. 2018 Jan 10;9(1):135. doi: 10.1038/s41467-017-02474-4. PMID:29321502[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Birschmann I, Stroobants AK, van den Berg M, Schafer A, Rosenkranz K, Kunau WH, Tabak HF. Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol Biol Cell. 2003 Jun;14(6):2226-36. Epub 2003 Mar 7. PMID:12808025 doi:http://dx.doi.org/10.1091/mbc.E02-11-0752
- ↑ Elgersma Y, Kwast L, van den Berg M, Snyder WB, Distel B, Subramani S, Tabak HF. Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S.cerevisiae, causes proliferation of the endoplasmic reticulum membrane. EMBO J. 1997 Dec 15;16(24):7326-41. doi: 10.1093/emboj/16.24.7326. PMID:9405362 doi:http://dx.doi.org/10.1093/emboj/16.24.7326
- ↑ 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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