7dde: Difference between revisions
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<StructureSection load='7dde' size='340' side='right'caption='[[7dde]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='7dde' size='340' side='right'caption='[[7dde]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7dde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dde OCA], [https://pdbe.org/7dde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dde RCSB], [https://www.ebi.ac.uk/pdbsum/7dde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dde ProSAT]</span></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=7dde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dde OCA], [https://pdbe.org/7dde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dde RCSB], [https://www.ebi.ac.uk/pdbsum/7dde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dde ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7dde" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7dde" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ye | [[Category: Ye K]] | ||
[[Category: Zhang | [[Category: Zhang J]] | ||
Latest revision as of 22:31, 29 May 2024
Cryo-EM structure of the Ape4 and Nbr1 complexCryo-EM structure of the Ape4 and Nbr1 complex
Structural highlights
Publication Abstract from PubMedIn selective autophagy, cargo selectivity is determined by autophagy receptors. However, it remains scarcely understood how autophagy receptors recognize specific protein cargos. In the fission yeast Schizosaccharomyces pombe, a selective autophagy pathway termed Nbr1-mediated vacuolar targeting (NVT) employs Nbr1, an autophagy receptor conserved across eukaryotes including humans, to target cytosolic hydrolases into the vacuole. Here, we identify two new NVT cargos, the mannosidase Ams1 and the aminopeptidase Ape4, that bind competitively to the first ZZ domain of Nbr1 (Nbr1-ZZ1). High-resolution cryo-EM analyses reveal how a single ZZ domain recognizes two distinct protein cargos. Nbr1-ZZ1 not only recognizes the N-termini of cargos via a conserved acidic pocket, similar to other characterized ZZ domains, but also engages additional parts of cargos in a cargo-specific manner. Our findings unveil a single-domain bispecific mechanism of autophagy cargo recognition, elucidate its underlying structural basis, and expand the understanding of ZZ domain-mediated protein-protein interactions. Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.,Wang YY, Zhang J, Liu XM, Li Y, Sui J, Dong MQ, Ye K, Du LL EMBO J. 2021 Jun 25:e107497. doi: 10.15252/embj.2020107497. PMID:34169534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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