5vxv: Difference between revisions
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New page: '''Unreleased structure''' The entry 5vxv is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Peroxisomal membrane protein PEX15== | |||
<StructureSection load='5vxv' size='340' side='right'caption='[[5vxv]], [[Resolution|resolution]] 1.55Å' 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]] 1.55Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </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]] | |||
Latest revision as of 04:53, 21 November 2024
Peroxisomal membrane protein PEX15
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