5e6o

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<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 ==
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<table><tr><td colspan='2'>[[5e6o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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://proteopedia.org/fgij/fg.htm?mol=5E6O FirstGlance]. <br>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e6n|5e6n]]</td></tr>
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</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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgg-2, ZK593.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6o ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5e6o" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Feng, W]]
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[[Category: Scheffersomyces stipitis]]
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[[Category: Qi, X]]
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[[Category: Feng W]]
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[[Category: Ren, J Q]]
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[[Category: Qi X]]
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[[Category: Wu, F]]
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[[Category: Ren JQ]]
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[[Category: Zhang, H]]
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[[Category: Wu F]]
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[[Category: Atg8 protein family]]
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[[Category: Zhang H]]
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[[Category: Protein binding-peptide complex]]
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[[Category: Ubiquitin-like protein]]
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Current revision

Crystal structure of C. elegans LGG-2 bound to an AIM/LIR motif

PDB ID 5e6o

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