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| | <StructureSection load='7lk3' size='340' side='right'caption='[[7lk3]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='7lk3' size='340' side='right'caption='[[7lk3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7lk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LK3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7lk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LK3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GABARAPL2, FLC3A, GEF2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=7lk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lk3 OCA], [https://pdbe.org/7lk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lk3 RCSB], [https://www.ebi.ac.uk/pdbsum/7lk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lk3 ProSAT]</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=7lk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lk3 OCA], [https://pdbe.org/7lk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lk3 RCSB], [https://www.ebi.ac.uk/pdbsum/7lk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lk3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GBRL2_HUMAN GBRL2_HUMAN]] Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.<ref>PMID:20418806</ref> <ref>PMID:23209295</ref>
| + | [https://www.uniprot.org/uniprot/GBRL2_HUMAN GBRL2_HUMAN] Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.<ref>PMID:20418806</ref> <ref>PMID:23209295</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Birkinshaw, R W]] | + | [[Category: Birkinshaw RW]] |
| - | [[Category: Czabotar, P E]] | + | [[Category: Czabotar PE]] |
| - | [[Category: Dewson, G]] | + | [[Category: Dewson G]] |
| - | [[Category: Scicluna, K]] | + | [[Category: Scicluna K]] |
| - | [[Category: Atg8 family]]
| + | |
| - | [[Category: Autophagosome]]
| + | |
| - | [[Category: Autophagy]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Ubiquitin-like]]
| + | |
| Structural highlights
Function
GBRL2_HUMAN Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.[1] [2]
Publication Abstract from PubMed
The Atg8 protein family comprises the GABA type A receptor-associated proteins (GABARAPs) and microtubule-associated protein 1 light chains 3 (MAP1LC3s) that are essential mediators of autophagy. The LC3-interacting region (LIR) motifs of autophagy receptors and adaptors bind Atg8 proteins to promote autophagosome formation, cargo recruitment, and autophagosome closure and fusion to lysosomes. A crystal structure of human GABARAPL2 has been published [PDB entry 4co7; Ma et al. (2015), Biochemistry, 54, 5469-5479]. This was crystallized in space group P21 with a monoclinic angle of 90 degrees and shows a pseudomerohedral twinning pathology. This article reports a new, untwinned GABARAPL2 crystal form, also in space group P21, but with a 98 degrees monoclinic angle. No major conformational differences were observed between the structures. In the structure described here, the C-terminal Phe117 binds into the LIR docking site (LDS) of a neighbouring molecule within the asymmetric unit, as observed in the previously reported structure. This crystal contact blocks the LDS for co-crystallization with ligands. Phe117 of GABARAPL2 is normally removed during biological processing by Atg4 family proteases. These data indicate that to establish interactions with the LIR, Phe117 should be removed to eliminate the crystal contact and liberate the LDS for co-crystallization with LIR peptides.
A new crystal form of GABARAPL2.,Scicluna K, Dewson G, Czabotar PE, Birkinshaw RW Acta Crystallogr F Struct Biol Commun. 2021 May 1;77(Pt 5):140-147. doi:, 10.1107/S2053230X21004489. Epub 2021 Apr 30. PMID:33949974[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z. LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J. 2010 Jun 2;29(11):1792-802. doi: 10.1038/emboj.2010.74. Epub 2010 Apr 23. PMID:20418806 doi:http://dx.doi.org/10.1038/emboj.2010.74
- ↑ Zhu Y, Massen S, Terenzio M, Lang V, Chen-Lindner S, Eils R, Novak I, Dikic I, Hamacher-Brady A, Brady NR. Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3 determines pro-survival mitophagy versus apoptosis. J Biol Chem. 2013 Jan 11;288(2):1099-113. doi: 10.1074/jbc.M112.399345. Epub 2012, Dec 3. PMID:23209295 doi:http://dx.doi.org/10.1074/jbc.M112.399345
- ↑ Scicluna K, Dewson G, Czabotar PE, Birkinshaw RW. A new crystal form of GABARAPL2. Acta Crystallogr F Struct Biol Commun. 2021 May 1;77(Pt 5):140-147. doi:, 10.1107/S2053230X21004489. Epub 2021 Apr 30. PMID:33949974 doi:http://dx.doi.org/10.1107/S2053230X21004489
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