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| | <StructureSection load='4arz' size='340' side='right'caption='[[4arz]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='4arz' size='340' side='right'caption='[[4arz]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4arz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ARZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4arz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4arz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arz OCA], [http://pdbe.org/4arz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4arz RCSB], [http://www.ebi.ac.uk/pdbsum/4arz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4arz 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=4arz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arz OCA], [https://pdbe.org/4arz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arz RCSB], [https://www.ebi.ac.uk/pdbsum/4arz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arz 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/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> | + | [[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. [[https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[GTP-binding protein|GTP-binding protein]] | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Jeong, J H]] | | [[Category: Jeong, J H]] |
| | [[Category: Kim, Y G]] | | [[Category: Kim, Y G]] |
| 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. [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.[1] [2]
Publication Abstract from PubMed
The heterodimeric Rag GTPases consisting of RagA (or RagB) and RagC (or RagD) are the key regulator activating the target of rapamycin complex 1 (TORC1) in response to the level of amino acids. The heterodimer between GTP-loaded RagA/B and GDP-loaded RagC/D is the most active form that binds Raptor and leads to the activation of TORC1. Here, we present the crystal structure of Gtr1p(GTP)-Gtr2p(GDP), the active yeast Rag GTPase heterodimer. The structure reveals that GTP-to-GDP conversion on Gtr2p results in a large conformational transition of this subunit, including a large scale rearrangement of a long segment whose corresponding region in RagA is involved in binding to Raptor. In addition, the two GTPase domains of the heterodimer are brought to contact with each other, but without causing any conformational change of the Gtr1p subunit. These features explain how the nucleotide-bound statuses of the two GTPases subunits switch the Raptor binding affinity on and off.
Crystal Structure of the Gtr1pGTP-Gtr2pGDP Protein Complex Reveals Large Structural Rearrangements Triggered by GTP-to-GDP Conversion.,Jeong JH, Lee KH, Kim YM, Kim DH, Oh BH, Kim YG J Biol Chem. 2012 Aug 24;287(35):29648-53. Epub 2012 Jul 17. PMID:22807443[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dubouloz F, Deloche O, Wanke V, Cameroni E, De Virgilio C. The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol Cell. 2005 Jul 1;19(1):15-26. PMID:15989961 doi:10.1016/j.molcel.2005.05.020
- ↑ Gao M, Kaiser CA. A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast. Nat Cell Biol. 2006 Jul;8(7):657-67. Epub 2006 May 28. PMID:16732272 doi:ncb1419
- ↑ Jeong JH, Lee KH, Kim YM, Kim DH, Oh BH, Kim YG. Crystal Structure of the Gtr1pGTP-Gtr2pGDP Protein Complex Reveals Large Structural Rearrangements Triggered by GTP-to-GDP Conversion. J Biol Chem. 2012 Aug 24;287(35):29648-53. Epub 2012 Jul 17. PMID:22807443 doi:http://dx.doi.org/10.1074/jbc.C112.384420
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