View source for 5vxv


==Peroxisomal membrane protein PEX15==
<StructureSection load='5vxv' size='340' side='right'caption='[[5vxv]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</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'>[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>
== Function ==
[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;">
== 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<ref>PMID:29321502</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vxv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Castanzo DT]]
[[Category: Gardner BM]]