6xmp

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Current revision (14:50, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6xmp' size='340' side='right'caption='[[6xmp]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='6xmp' size='340' side='right'caption='[[6xmp]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6xmp]] 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=6XMP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XMP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6xmp]] 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=6XMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XMP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xmp OCA], [http://pdbe.org/6xmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xmp RCSB], [http://www.ebi.ac.uk/pdbsum/6xmp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xmp ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6xmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xmp OCA], [https://pdbe.org/6xmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xmp RCSB], [https://www.ebi.ac.uk/pdbsum/6xmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xmp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ATC6_YEAST ATC6_YEAST]] Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis.<ref>PMID:24392018</ref>
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[https://www.uniprot.org/uniprot/SPF1_YEAST SPF1_YEAST] Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (PubMed:22918956, PubMed:32973005). Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (PubMed:32973005). Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (PubMed:32973005).<ref>PMID:22918956</ref> <ref>PMID:32973005</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Organelle identity depends on protein composition. How mistargeted proteins are selectively recognized and removed from organelles is incompletely understood. Here, we found that the orphan P5A-adenosine triphosphatase (ATPase) transporter ATP13A1 (Spf1 in yeast) directly interacted with the transmembrane segment (TM) of mitochondrial tail-anchored proteins. P5A-ATPase activity mediated the extraction of mistargeted proteins from the endoplasmic reticulum (ER). Cryo-electron microscopy structures of Saccharomyces cerevisiae Spf1 revealed a large, membrane-accessible substrate-binding pocket that alternately faced the ER lumen and cytosol and an endogenous substrate resembling an alpha-helical TM. Our results indicate that the P5A-ATPase could dislocate misinserted hydrophobic helices flanked by short basic segments from the ER. TM dislocation by the P5A-ATPase establishes an additional class of P-type ATPase substrates and may correct mistakes in protein targeting or topogenesis.
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The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase.,McKenna MJ, Sim SI, Ordureau A, Wei L, Harper JW, Shao S, Park E Science. 2020 Sep 25;369(6511). pii: 369/6511/eabc5809. doi:, 10.1126/science.abc5809. PMID:32973005<ref>PMID:32973005</ref>
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6xmp" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Park, E]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Sim, S I]]
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[[Category: Park E]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Sim SI]]
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[[Category: P-type atpase]]
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[[Category: Protein quality control]]
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[[Category: Transmembrane helix dislocase]]
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[[Category: Transport protein]]
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Current revision

Structure of P5A-ATPase Spf1, Apo form

PDB ID 6xmp

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