6aag
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of budding yeast Atg8 complexed with the helical AIM of Hfl1.== | |
| + | <StructureSection load='6aag' size='340' side='right' caption='[[6aag]], [[Resolution|resolution]] 2.44Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6aag]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AAG FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aag OCA], [http://pdbe.org/6aag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aag RCSB], [http://www.ebi.ac.uk/pdbsum/6aag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aag ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular beta-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding. | ||
| - | + | Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein.,Liu XM, Yamasaki A, Du XM, Coffman VC, Ohsumi Y, Nakatogawa H, Wu JQ, Noda NN, Du LL Elife. 2018 Nov 19;7. pii: 41237. doi: 10.7554/eLife.41237. PMID:30451685<ref>PMID:30451685</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6aag" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Noda, N N]] | ||
| + | [[Category: Yamasaki, A]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Vacuole autophagy]] | ||
Revision as of 06:41, 12 December 2018
Crystal structure of budding yeast Atg8 complexed with the helical AIM of Hfl1.
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