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| | <StructureSection load='5wrd' size='340' side='right'caption='[[5wrd]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5wrd' size='340' side='right'caption='[[5wrd]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wrd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wrd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WRD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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">Map1lc3b, Map1alc3, Map1lc3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrd OCA], [http://pdbe.org/5wrd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrd RCSB], [http://www.ebi.ac.uk/pdbsum/5wrd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrd 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=5wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrd OCA], [https://pdbe.org/5wrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wrd RCSB], [https://www.ebi.ac.uk/pdbsum/5wrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MLP3B_MOUSE MLP3B_MOUSE]] Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). 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. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.[UniProtKB:Q9GZQ8] [[http://www.uniprot.org/uniprot/FYCO1_MOUSE FYCO1_MOUSE]] May mediate microtubule plus end-directed vesicle transport. | + | [https://www.uniprot.org/uniprot/MLP3B_MOUSE MLP3B_MOUSE] Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). 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. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.[UniProtKB:Q9GZQ8] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ohto, U]] | + | [[Category: Ohto U]] |
| - | [[Category: Sakurai, S]] | + | [[Category: Sakurai S]] |
| - | [[Category: Shimizu, T]] | + | [[Category: Shimizu T]] |
| - | [[Category: Autophagy]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
MLP3B_MOUSE Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). 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. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.[UniProtKB:Q9GZQ8]
Publication Abstract from PubMed
FYVE and coiled-coil domain-containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus-end-directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3-phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3-interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N-terminal and C-terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species.
The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif.,Sakurai S, Tomita T, Shimizu T, Ohto U Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):130-137. doi:, 10.1107/S2053230X17001911. Epub 2017 Feb 21. PMID:28291748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sakurai S, Tomita T, Shimizu T, Ohto U. The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif. Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):130-137. doi:, 10.1107/S2053230X17001911. Epub 2017 Feb 21. PMID:28291748 doi:http://dx.doi.org/10.1107/S2053230X17001911
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