4fuw

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==Crystal structure of Ego3 mutant==
==Crystal structure of Ego3 mutant==
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<StructureSection load='4fuw' size='340' side='right' caption='[[4fuw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='4fuw' size='340' side='right'caption='[[4fuw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fuw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FUW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fuw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FUW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ftx|4ftx]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLM4, EGO3, GSE1, YBR077C, YBR0723 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4fuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fuw OCA], [https://pdbe.org/4fuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fuw RCSB], [https://www.ebi.ac.uk/pdbsum/4fuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fuw 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fuw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fuw RCSB], [http://www.ebi.ac.uk/pdbsum/4fuw PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SLM4_YEAST SLM4_YEAST] Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Component of the EGO complex, a complex involved in the regulation of microautophagy.<ref>PMID:15989961</ref> <ref>PMID:16732272</ref>
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The yeast EGO complex, consisting of Gtr1, Gtr2, Ego1, and Ego3, localizes to the endosomal and vacuolar membranes and plays a pivotal role in cell growth and autophagy regulation through relaying amino acid signals to activate TORC1. Here, we report the crystal structures of a wild-type and a mutant form of Saccharomyces cerevisiae Ego3. Ego3 assumes a homodimeric structure similar to that of the mammalian MP1-p14 heterodimer and the C-terminal domains of the yeast Gtr1-Gtr2 heterodimer, both of which function in TORC1 signaling. Structural and genetic data demonstrate that the unique dimer conformation of Ego3 is essential for the integrity and function of the EGO complex. Structural and functional data also identify a potential binding site for Gtr1-Gtr2. These results suggest a structural conservation of the protein components involved in amino acid signaling to TORC1 and reveal structural insights into the molecular mechanism of Ego3 function in TORC1 signaling.
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Ego3 Functions as a Homodimer to Mediate the Interaction between Gtr1-Gtr2 and Ego1 in the EGO Complex to Activate TORC1.,Zhang T, Peli-Gulli MP, Yang H, De Virgilio C, Ding J Structure. 2012 Oct 30. pii: S0969-2126(12)00372-3. doi:, 10.1016/j.str.2012.09.019. PMID:23123112<ref>PMID:23123112</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Large Structures]]
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[[Category: Ding, J]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Peli-Gulli, M P]]
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[[Category: De Virgilio C]]
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[[Category: Virgilio, C De]]
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[[Category: Ding J]]
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[[Category: Yang, H]]
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[[Category: Peli-Gulli MP]]
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[[Category: Zhang, T]]
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[[Category: Yang H]]
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[[Category: Ego complex]]
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[[Category: Zhang T]]
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[[Category: Ego3]]
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[[Category: Protein binding]]
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[[Category: Tor signaling]]
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Current revision

Crystal structure of Ego3 mutant

PDB ID 4fuw

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