View source for 9vbs


==Crystal structure of the coiled-coil of ALLO-1a==
<StructureSection load='9vbs' size='340' side='right'caption='[[9vbs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vbs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VBS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.401&#8491;</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=9vbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vbs OCA], [https://pdbe.org/9vbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vbs RCSB], [https://www.ebi.ac.uk/pdbsum/9vbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vbs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALLO1_CAEEL ALLO1_CAEEL] Autophagy receptor, which is required for allophagy, an autophagic process in which paternal organelles, including mitochondria and membranous organelles, are degraded in early embryos. After fertilization, recruited to ubiquitin-modified paternal organelles and is required for the formation of autophagosomes around the paternal organelles. Also plays a role in the regulation of autophagy in germ cells.<ref>PMID:29255173</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the nematode Caenorhabditis elegans, sperm-derived mitochondria and membranous organelles (MOs) are selectively degraded by autophagy in embryos in a process termed allophagy. For this process, ALLO-1 functions as an autophagy adaptor. The allo-1 gene encodes two splice isoforms, ALLO-1a and b, which have different C-terminal sequences and are predominantly targeted to MOs and paternal mitochondria, respectively. However, the mechanism by which ALLO-1 targets the paternal organelles remains unknown. In this study, X-ray crystallography analysis reveals that the C-terminal region of ALLO-1a forms a parallel coiled-coil structure. In addition, Alphafold-Multimer predicts that this region directly interacts with ubiquitin. We showed that ALLO-1a interacts with K48- and K63-linked polyubiquitin in vitro and found that the 355th Asp residue of ALLO-1a at the predicted interface with ubiquitin is important for its ubiquitin binding in vitro and also for its MO-targeting and MO degradation in embryos. These results suggest that ubiquitin is a marker for the recognition of MOs by the autophagy machinery in C. elegans embryos.

ALLO-1a is a ubiquitin-binding adaptor for allophagy in Caenorhabditis elegans.,Norizuki T, Kushida Y, Sekimoto T, Sasaki T, Yamano K, Matsuda N, Sasaki R, Noda NN, Sato K, Sato M J Cell Sci. 2025 Nov 14:jcs.264252. doi: 10.1242/jcs.264252. PMID:41234204<ref>PMID:41234204</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vbs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Noda NN]]