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The | ==Structure of the S. cerevisiae alpha-mannosidase 1== | ||
<SX load='5jm0' size='340' side='right' viewer='molstar' caption='[[5jm0]], [[Resolution|resolution]] 6.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jm0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JM0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.3Å</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=5jm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jm0 OCA], [https://pdbe.org/5jm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jm0 RCSB], [https://www.ebi.ac.uk/pdbsum/5jm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jm0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MAN1_YEAST MAN1_YEAST] Degrades free oligosaccharides in the vacuole.<ref>PMID:12723970</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Selective autophagy is the mechanism by which large cargos are specifically sequestered for degradation. The structural details of cargo and receptor assembly giving rise to autophagic vesicles remain to be elucidated. We utilize the yeast cytoplasm-to-vacuole targeting (Cvt) pathway, a prototype of selective autophagy, together with a multi-scale analysis approach to study the molecular structure of Cvt vesicles. We report the oligomeric nature of the major Cvt cargo Ape1 with a combined 2.8 A X-ray and negative stain EM structure, as well as the secondary cargo Ams1 with a 6.3 A cryo-EM structure. We show that the major dodecameric cargo prApe1 exhibits a tendency to form higher-order chain structures that are broken upon interaction with the receptor Atg19 in vitro The stoichiometry of these cargo-receptor complexes is key to maintaining the size of the Cvt aggregate in vivo Using correlative light and electron microscopy, we further visualize key stages of Cvt vesicle biogenesis. Our findings suggest that Atg19 interaction limits Ape1 aggregate size while serving as a vehicle for vacuolar delivery of tetrameric Ams1. | |||
Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.,Bertipaglia C, Schneider S, Jakobi AJ, Tarafder AK, Bykov YS, Picco A, Kukulski W, Kosinski J, Hagen WJ, Ravichandran AC, Wilmanns M, Kaksonen M, Briggs JA, Sachse C EMBO Rep. 2016 Jun 6. pii: e201541960. PMID:27266708<ref>PMID:27266708</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5jm0" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Mannosidase 3D structures|Mannosidase 3D structures]] | ||
[[Category: Sachse | == References == | ||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Hagen WJH]] | |||
[[Category: Jakobi AJ]] | |||
[[Category: Kosinski J]] | |||
[[Category: Sachse C]] | |||
[[Category: Schneider S]] | |||
Latest revision as of 21:58, 20 September 2023
Structure of the S. cerevisiae alpha-mannosidase 1Structure of the S. cerevisiae alpha-mannosidase 1
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