6jwp

From Proteopedia

(Difference between revisions)

Revision as of 15:05, 11 December 2019

crystal structure of EGOC

Structural highlights

6jwp is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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. [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.^[1] ^[2] [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.^[3] ^[4] [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.^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6jwp"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6jwp is ON HOLD  until Paper Publication
+==crystal structure of EGOC==
+<StructureSection load='6jwp' size='340' side='right'caption='[[6jwp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== 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>
+</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>
+<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>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Zhang, T., Ding, J.
+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<ref>PMID:31579828</ref>
-Description: crystal structure of EGOC
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6jwp" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Ding, J]]
 [[Category: Zhang, T]]
+[[Category: Egoc]]
+[[Category: Gtr1]]
+[[Category: Protein transport]]
+[[Category: Roadblock domain]]
+[[Category: Torc1]]

6jwp

From Proteopedia

Revision as of 15:05, 11 December 2019

crystal structure of EGOC

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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