5e6o: Difference between revisions

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==Crystal structure of C. elegans LGG-2 bound to an AIM/LIR motif==
==Crystal structure of C. elegans LGG-2 bound to an AIM/LIR motif==
<StructureSection load='5e6o' size='340' side='right' caption='[[5e6o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='5e6o' size='340' side='right'caption='[[5e6o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e6o]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6O FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e6o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [https://en.wikipedia.org/wiki/Scheffersomyces_stipitis Scheffersomyces stipitis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E6O FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e6n|5e6n]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=5e6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6o OCA], [http://pdbe.org/5e6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6o RCSB], [http://www.ebi.ac.uk/pdbsum/5e6o PDBsum]</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=5e6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6o OCA], [https://pdbe.org/5e6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e6o RCSB], [https://www.ebi.ac.uk/pdbsum/5e6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LGG2_CAEEL LGG2_CAEEL]] Ubiquitin-like modifier involved in autophagy and essential for dauer development and life-span extension.<ref>PMID:20523114</ref> 
[https://www.uniprot.org/uniprot/LGG2_CAEEL LGG2_CAEEL] Ubiquitin-like modifier involved in autophagy and essential for dauer development and life-span extension.<ref>PMID:20523114</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multicellular organisms have multiple homologs of the yeast ATG8 gene, but the differential roles of these homologs in autophagy during development remain largely unknown. Here we investigated structure/function relationships in the two C. elegans Atg8 homologs, LGG-1 and LGG-2. lgg-1 is essential for degradation of protein aggregates, while lgg-2 has cargo-specific and developmental-stage-specific roles in aggregate degradation. Crystallography revealed that the N-terminal tails of LGG-1 and LGG-2 adopt the closed and open form, respectively. LGG-1 and LGG-2 interact differentially with autophagy substrates and Atg proteins, many of which carry a LIR motif. LGG-1 and LGG-2 have structurally distinct substrate binding pockets that prefer different residues in the interacting LIR motif, thus influencing binding specificity. Lipidated LGG-1 and LGG-2 possess distinct membrane tethering and fusion activities, which may result from the N-terminal differences. Our study reveals the differential function of two ATG8 homologs in autophagy during C. elegans development.
 
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.,Wu F, Watanabe Y, Guo XY, Qi X, Wang P, Zhao HY, Wang Z, Fujioka Y, Zhang H, Ren JQ, Fang TC, Shen YX, Feng W, Hu JJ, Noda NN, Zhang H Mol Cell. 2015 Dec 17;60(6):914-29. doi: 10.1016/j.molcel.2015.11.019. PMID:26687600<ref>PMID:26687600</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e6o" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Feng, W]]
[[Category: Caenorhabditis elegans]]
[[Category: Qi, X]]
[[Category: Large Structures]]
[[Category: Ren, J Q]]
[[Category: Scheffersomyces stipitis]]
[[Category: Wu, F]]
[[Category: Feng W]]
[[Category: Zhang, H]]
[[Category: Qi X]]
[[Category: Atg8 protein family]]
[[Category: Ren JQ]]
[[Category: Protein binding-peptide complex]]
[[Category: Wu F]]
[[Category: Ubiquitin-like protein]]
[[Category: Zhang H]]
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