7jlp

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Current revision (11:02, 23 October 2024) (edit) (undo)
 
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<StructureSection load='7jlp' size='340' side='right'caption='[[7jlp]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='7jlp' size='340' side='right'caption='[[7jlp]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7jlp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JLP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JLP FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JLP 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=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</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]] 3.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG9A, APG9L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene></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=7jlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jlp OCA], [http://pdbe.org/7jlp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jlp RCSB], [http://www.ebi.ac.uk/pdbsum/7jlp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jlp ProSAT]</span></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=7jlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jlp OCA], [https://pdbe.org/7jlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jlp RCSB], [https://www.ebi.ac.uk/pdbsum/7jlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jlp ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[http://www.uniprot.org/uniprot/ATG9A_HUMAN ATG9A_HUMAN]] Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H.<ref>PMID:16940348</ref>
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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De novo formation of the double-membrane compartment autophagosome is seeded by small vesicles carrying membrane protein autophagy-related 9 (ATG9), the function of which remains unknown. Here we find that ATG9A scrambles phospholipids of membranes in vitro. Cryo-EM structures of human ATG9A reveal a trimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Similarities to ABC exporters suggest that ATG9A could be a transporter that uses the central pore to function. Moreover, molecular dynamics simulation suggests that the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipids to flip. Mutations in the pore reduce scrambling activity and yield markedly smaller autophagosomes, indicating that lipid scrambling by ATG9A is essential for membrane expansion. We propose ATG9A acts as a membrane-embedded funnel to facilitate lipid flipping and to redistribute lipids added to the outer leaflet of ATG9 vesicles, thereby enabling growth into autophagosomes.
 
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Structure, lipid scrambling activity and role in autophagosome formation of ATG9A.,Maeda S, Yamamoto H, Kinch LN, Garza CM, Takahashi S, Otomo C, Grishin NV, Forli S, Mizushima N, Otomo T Nat Struct Mol Biol. 2020 Oct 26. pii: 10.1038/s41594-020-00520-2. doi:, 10.1038/s41594-020-00520-2. PMID:33106659<ref>PMID:33106659</ref>
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==See Also==
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*[[Autophagy-related protein 3D structures|Autophagy-related protein 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 7jlp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Maeda, S]]
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[[Category: Maeda S]]
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[[Category: Otomo, T]]
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[[Category: Otomo T]]
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[[Category: Autophagy]]
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[[Category: Membrane protein]]
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Current revision

cryo-EM structure of human ATG9A in nanodiscs

PDB ID 7jlp

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