2kzb
From Proteopedia
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| - | {{STRUCTURE_2kzb| PDB=2kzb | SCENE= }} | ||
| - | ===Solution structure of alpha-mannosidase binding domain of Atg19=== | ||
| - | {{ABSTRACT_PUBMED_20659891}} | ||
| - | == | + | ==Solution structure of alpha-mannosidase binding domain of Atg19== |
| - | [[http://www.uniprot.org/uniprot/ATG19_YEAST ATG19_YEAST | + | <StructureSection load='2kzb' size='340' side='right'caption='[[2kzb]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2kzb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KZB FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kzb OCA], [https://pdbe.org/2kzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kzb RCSB], [https://www.ebi.ac.uk/pdbsum/2kzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kzb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATG19_YEAST ATG19_YEAST] Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth.<ref>PMID:11382752</ref> <ref>PMID:11430817</ref> <ref>PMID:12479807</ref> <ref>PMID:12479808</ref> <ref>PMID:15138258</ref> <ref>PMID:15801807</ref> <ref>PMID:16186126</ref> <ref>PMID:15659643</ref> <ref>PMID:17132049</ref> <ref>PMID:17700056</ref> <ref>PMID:17192412</ref> <ref>PMID:17238920</ref> <ref>PMID:19061865</ref> <ref>PMID:21228276</ref> <ref>PMID:19021777</ref> <ref>PMID:20659891</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In the yeast Saccharomyces cerevisiae, a precursor form of aminopeptidase I (prApe1) and alpha-mannosidase (Ams1) are selectively transported to the vacuole through the cytoplasm-to-vacuole targeting pathway under vegetative conditions and through autophagy under starvation conditions. Atg19 plays a central role in these processes by linking Ams1 and prApe1 to Atg8 and Atg11. However, little is known about the molecular mechanisms of cargo recognition by Atg19. Here, we report structural and functional analyses of Atg19 and its paralog, Atg34. A protease-resistant domain was identified in the C-terminal region of Atg19, which was also conserved in Atg34. In vitro pulldown assays showed that the C-terminal domains of both Atg19 and Atg34 are responsible for Ams1 binding; these domains are hereafter referred to as Ams1-binding domains (ABDs). The transport of Ams1, but not prApe1, was blocked in atg19Deltaatg34Delta cells expressing Atg19(DeltaABD), indicating that ABD is specifically required for Ams1 transport. We then determined the solution structures of the ABDs of Atg19 and Atg34 using NMR spectroscopy. Both ABD structures have a canonical immunoglobulin fold consisting of eight beta-strands with highly conserved loops clustered at one side of the fold. These facts, together with the results of a mutational analysis, suggest that ABD recognizes Ams1 using these conserved loops. | ||
| - | + | Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34.,Watanabe Y, Noda NN, Kumeta H, Suzuki K, Ohsumi Y, Inagaki F J Biol Chem. 2010 Sep 24;285(39):30026-33. Epub 2010 Jul 21. PMID:20659891<ref>PMID:20659891</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2kzb" style="background-color:#fffaf0;"></div> |
| - | [[Category: Inagaki | + | |
| - | [[Category: Kumeta | + | ==See Also== |
| - | [[Category: Noda | + | *[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]] |
| - | [[Category: Ohsumi | + | == References == |
| - | [[Category: Suzuki | + | <references/> |
| - | [[Category: Watanabe | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Saccharomyces cerevisiae]] | |
| - | + | [[Category: Inagaki F]] | |
| + | [[Category: Kumeta H]] | ||
| + | [[Category: Noda N]] | ||
| + | [[Category: Ohsumi Y]] | ||
| + | [[Category: Suzuki K]] | ||
| + | [[Category: Watanabe Y]] | ||
Current revision
Solution structure of alpha-mannosidase binding domain of Atg19
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