5azg: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 5azg is ~~ON HOLD~~

==Crystal structure of LGG-1 complexed with a UNC-51 peptide==

== Structural highlights ==

<table><tr><td colspan='2'>[[5azg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZG FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=5azg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azg OCA], [https://pdbe.org/5azg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5azg RCSB], [https://www.ebi.ac.uk/pdbsum/5azg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5azg ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/LGG1_CAEEL LGG1_CAEEL] Ubiquitin-like modifier involved in autophagy and essential for dauer development and life-span extension (PubMed:12958363, PubMed:20523114). Plays a role in mitophagy (PubMed:25896323).<ref>PMID:12958363</ref> <ref>PMID:20523114</ref> <ref>PMID:25896323</ref>

== 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.

~~Authors:~~ Watanabe, Y., ~~Fujioka~~, Y., Noda, N.N.

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Fujioka, Y]]

[[Category: ~~Watanabe, Y~~]]

== References ==

[[Category: ~~Noda, N.N~~]]

__TOC__

</StructureSection>

[[Category: Caenorhabditis elegans]]

[[Category: Large Structures]]

[[Category: Fujioka Y]]

[[Category: Noda NN]]

[[Category: Watanabe Y]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5azg is ON HOLD
+==Crystal structure of LGG-1 complexed with a UNC-51 peptide==
+<StructureSection load='5azg' size='340' side='right'caption='[[5azg]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5azg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZG FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=5azg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azg OCA], [https://pdbe.org/5azg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5azg RCSB], [https://www.ebi.ac.uk/pdbsum/5azg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5azg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LGG1_CAEEL LGG1_CAEEL] Ubiquitin-like modifier involved in autophagy and essential for dauer development and life-span extension (PubMed:12958363, PubMed:20523114). Plays a role in mitophagy (PubMed:25896323).<ref>PMID:12958363</ref> <ref>PMID:20523114</ref> <ref>PMID:25896323</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.
-Authors: Watanabe, Y., Fujioka, Y., Noda, N.N.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Fujioka, Y]]
+<div class="pdbe-citations 5azg" style="background-color:#fffaf0;"></div>
-[[Category: Watanabe, Y]]
+== References ==
-[[Category: Noda, N.N]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Caenorhabditis elegans]]
+[[Category: Large Structures]]
+[[Category: Fujioka Y]]
+[[Category: Noda NN]]
+[[Category: Watanabe Y]]