5azg

From Proteopedia

(Difference between revisions)

Revision as of 08:50, 1 January 2020

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

Structural highlights

5azg is a 4 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5azf, 5azh
Gene:	lgg-1, C32D5.9 (CAEEL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] ^[3] [UNC51_CAEEL] Protein kinase important for axonal elongation and axonal guidance. Functions in the CAN axons to direct both anterior and posterior migrations. Phosphorylates both unc-14 and vab-8.^[4] ^[5]

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^[6]

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

References

↑ Melendez A, Talloczy Z, Seaman M, Eskelinen EL, Hall DH, Levine B. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science. 2003 Sep 5;301(5638):1387-91. PMID:12958363 doi:http://dx.doi.org/10.1126/science.1087782
↑ Alberti A, Michelet X, Djeddi A, Legouis R. The autophagosomal protein LGG-2 acts synergistically with LGG-1 in dauer formation and longevity in C. elegans. Autophagy. 2010 Jul;6(5):622-33. doi: 10.4161/auto.6.5.12252. Epub 2010 Jul 1. PMID:20523114 doi:http://dx.doi.org/10.4161/auto.6.5.12252
↑ Palikaras K, Lionaki E, Tavernarakis N. Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans. Nature. 2015 May 28;521(7553):525-8. doi: 10.1038/nature14300. Epub 2015 Apr 20. PMID:25896323 doi:http://dx.doi.org/10.1038/nature14300
↑ Lai T, Garriga G. The conserved kinase UNC-51 acts with VAB-8 and UNC-14 to regulate axon outgrowth in C. elegans. Development. 2004 Dec;131(23):5991-6000. PMID:15539493 doi:http://dx.doi.org/10.1242/dev.01457
↑ Ogura K, Wicky C, Magnenat L, Tobler H, Mori I, Muller F, Ohshima Y. Caenorhabditis elegans unc-51 gene required for axonal elongation encodes a novel serine/threonine kinase. Genes Dev. 1994 Oct 15;8(20):2389-400. PMID:7958904
↑ 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. Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy. Mol Cell. 2015 Dec 17;60(6):914-29. doi: 10.1016/j.molcel.2015.11.019. PMID:26687600 doi:http://dx.doi.org/10.1016/j.molcel.2015.11.019

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5azg"

@@ Line 1: / Line 1: @@
 ==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=''>
+<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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5azg]] is a 4 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=5AZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZG FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5azf|5azf]], [[5azh|5azh]]</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=5azg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azg OCA], [http://pdbe.org/5azg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azg RCSB], [http://www.ebi.ac.uk/pdbsum/5azg PDBsum]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgg-1, C32D5.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=5azg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azg OCA], [http://pdbe.org/5azg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azg RCSB], [http://www.ebi.ac.uk/pdbsum/5azg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azg ProSAT]</span></td></tr>
 </table>
 == Function ==
 [[http://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>  [[http://www.uniprot.org/uniprot/UNC51_CAEEL UNC51_CAEEL]] Protein kinase important for axonal elongation and axonal guidance. Functions in the CAN axons to direct both anterior and posterior migrations. Phosphorylates both unc-14 and vab-8.<ref>PMID:15539493</ref> <ref>PMID:7958904</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 5azg" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Caeel]]
+[[Category: Large Structures]]
 [[Category: Fujioka, Y]]
 [[Category: Noda, N N]]

5azg

From Proteopedia

Revision as of 08:50, 1 January 2020

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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