5vxv
From Proteopedia
(Difference between revisions)
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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. 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 [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> |
</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='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'>[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> | ||
</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> | [[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> | ||
| + | <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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5vxv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Castanzo, D T]] | [[Category: Castanzo, D T]] | ||
[[Category: Gardner, B M]] | [[Category: Gardner, B M]] | ||
[[Category: Alpha helical]] | [[Category: Alpha helical]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 20:49, 24 January 2018
Peroxisomal membrane protein PEX15
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