View source for 5wlp


==Solution structure of the pseudo-receiver domain of Atg32==
<StructureSection load='5wlp' size='340' side='right'caption='[[5wlp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wlp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WLP FirstGlance]. <br>
</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=5wlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wlp OCA], [https://pdbe.org/5wlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wlp RCSB], [https://www.ebi.ac.uk/pdbsum/5wlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wlp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATG32_YEAST ATG32_YEAST] Mitophagy-specific receptor that recruits the autophagic machinery to mitochondria and regulates selective degradation of mitochondria. Mitophagy contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Recruits ATG11 to the surface of mitochondria. Promotes also autophagy-dependent peroxisome degradation.<ref>PMID:19770589</ref> <ref>PMID:19619494</ref> <ref>PMID:19619495</ref> <ref>PMID:19793921</ref> <ref>PMID:21576396</ref> <ref>PMID:22914317</ref> <ref>PMID:22643220</ref> <ref>PMID:22157017</ref> <ref>PMID:22308029</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondria are targeted for degradation by mitophagy, a selective form of autophagy. In Saccharomyces cerevisiae, mitophagy is dependent on the autophagy receptor, Atg32, an outer mitochondrial membrane protein. Once activated, Atg32 recruits the autophagy machinery to mitochondria, facilitating mitochondrial capture in phagophores, the precursors to autophagosomes. However, the mechanism of Atg32 activation remains poorly understood. To investigate this crucial step in mitophagy regulation, we examined the structure of Atg32. We have identified a structured domain in Atg32 that is essential for the initiation of mitophagy, as it is required for the proteolysis of the C-terminal domain of Atg32 and the subsequent recruitment of Atg11. The solution structure of this domain was determined by NMR spectroscopy, revealing that Atg32 contains a previously undescribed pseudo-receiver (PsR) domain. Our data suggests that the PsR domain of Atg32 regulates Atg32 activation and the initiation of mitophagy.

A Pseudo-Receiver Domain in Atg32 is Required for Mitophagy.,Xia X, Katzenell S, Reinhart EF, Bauer KM, Pellegrini M, Ragusa MJ Autophagy. 2018 Jun 16. doi: 10.1080/15548627.2018.1472838. PMID:29909755<ref>PMID:29909755</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wlp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Pellegrini M]]
[[Category: Ragusa MJ]]
[[Category: Xue X]]