4edj

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4edj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4edj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.901&#8491;</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=K:POTASSIUM+ION'>K</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=4edj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edj OCA], [https://pdbe.org/4edj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edj RCSB], [https://www.ebi.ac.uk/pdbsum/4edj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edj 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=4edj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edj OCA], [https://pdbe.org/4edj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edj RCSB], [https://www.ebi.ac.uk/pdbsum/4edj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GORS2_HUMAN GORS2_HUMAN]] Plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA.<ref>PMID:10487747</ref> <ref>PMID:21515684</ref>
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[https://www.uniprot.org/uniprot/GORS2_HUMAN GORS2_HUMAN] Plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA.<ref>PMID:10487747</ref> <ref>PMID:21515684</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mitotic phosphorylation of the conserved GRASP domain of GRASP65 disrupts its self-association leading to a loss of Golgi membrane tethering, cisternal unlinking and Golgi breakdown. Recently the structural basis of the GRASP self-interaction was determined, yet the mechanism by which phosphorylation disrupts this activity is unknown. Here we present the crystal structure of a GRASP phosphomimic containing an aspartic acid substitution for a serine residue (Ser189) that in GRASP65 is phosphorylated by Polo-like kinase I causing a block in membrane tethering and Golgi ribbon formation. The structure revealed a conformational change in the GRASP internal ligand that prevented its insertion into the PDZ binding pocket and gel filtration assays showed that this phosphomimetic mutant exhibited a significant reduction in dimer formation. Interestingly, the structure also revealed an apparent propagation of conformational change from the site of phosphorylation to the shifted ligand and alanine substitution of two residues (Glu145 and Ser146) at penultimate positions in this chain rescued dimer formation by the phosphomimic. These data reveal the structural basis of the phosphoinhibition of GRASP-mediated membrane tethering and provide a mechanism for its allosteric regulation.
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Allosteric regulation of GRASP-dependent Golgi membrane tethering by mitotic phosphorylation.,Truschel ST, Zhang M, Bachert C, Macbeth MR, Linstedt AD J Biol Chem. 2012 Apr 20. PMID:22523075<ref>PMID:22523075</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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<div class="pdbe-citations 4edj" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of the GRASP55 GRASP Domain with a phosphomimetic mutation (S189D)

PDB ID 4edj

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