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| | <StructureSection load='6jwp' size='340' side='right'caption='[[6jwp]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='6jwp' size='340' side='right'caption='[[6jwp]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jwp]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JWP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jwp]] is a 10 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=6JWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JWP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.2Å</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=6jwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jwp OCA], [http://pdbe.org/6jwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jwp RCSB], [http://www.ebi.ac.uk/pdbsum/6jwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jwp ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6jwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jwp OCA], [https://pdbe.org/6jwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jwp RCSB], [https://www.ebi.ac.uk/pdbsum/6jwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jwp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GTR1_YEAST GTR1_YEAST]] GTPase component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Functionally associated with the inorganic phosphate transporter PHO84. It is probably required for modulation of PHO84 or involved in its intracellular localization. [[http://www.uniprot.org/uniprot/MEH1_YEAST MEH1_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> [[http://www.uniprot.org/uniprot/GTR2_YEAST GTR2_YEAST]] GTPase. 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> [[http://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> | + | [https://www.uniprot.org/uniprot/GTR1_YEAST GTR1_YEAST] GTPase component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Functionally associated with the inorganic phosphate transporter PHO84. It is probably required for modulation of PHO84 or involved in its intracellular localization. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6jwp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6jwp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ding, J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Zhang, T]] | + | [[Category: Ding J]] |
| - | [[Category: Egoc]] | + | [[Category: Zhang T]] |
| - | [[Category: Gtr1]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Roadblock domain]]
| + | |
| - | [[Category: Torc1]]
| + | |
| Structural highlights
Function
GTR1_YEAST GTPase component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Functionally associated with the inorganic phosphate transporter PHO84. It is probably required for modulation of PHO84 or involved in its intracellular localization.
Publication Abstract from PubMed
The Rag/Gtr GTPases serve as a central module in the nutrient-sensing signaling network upstream of TORC1. In yeast, the anchoring of Gtr1-Gtr2 to membranes depends on the Ego1-Ego2-Ego3 ternary complex (EGO-TC), resulting in an EGO-TC-Gtr1-Gtr2 complex (EGOC). EGO-TC and human Ragulator share no obvious sequence similarities and also differ in their composition with respect to the number of known subunits, which raises the question of how the EGO-TC fulfills its function in recruiting Gtr1-Gtr2. Here, we report the structure of EGOC, in which Ego1 wraps around Ego2, Ego3, and Gtr1-Gtr2. In addition, Ego3 interacts with Gtr1-Gtr2 to stabilize the complex. The functional roles of key residues involved in the assembly are validated by in vivo assays. Our structural and functional data combined demonstrate that EGOC and Ragulator-Rag complex are structurally conserved and that EGO-TC is essential and sufficient to recruit Gtr1-Gtr2 to membranes to ensure appropriate TORC1 signaling.
Structural insights into the EGO-TC-mediated membrane tethering of the TORC1-regulatory Rag GTPases.,Zhang T, Peli-Gulli MP, Zhang Z, Tang X, Ye J, De Virgilio C, Ding J Sci Adv. 2019 Sep 25;5(9):eaax8164. doi: 10.1126/sciadv.aax8164. eCollection 2019, Sep. PMID:31579828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang T, Peli-Gulli MP, Zhang Z, Tang X, Ye J, De Virgilio C, Ding J. Structural insights into the EGO-TC-mediated membrane tethering of the TORC1-regulatory Rag GTPases. Sci Adv. 2019 Sep 25;5(9):eaax8164. doi: 10.1126/sciadv.aax8164. eCollection 2019, Sep. PMID:31579828 doi:http://dx.doi.org/10.1126/sciadv.aax8164
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