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| | ==Crystal Structure of GRASP55 GRASP domain (residues 7-208)== | | ==Crystal Structure of GRASP55 GRASP domain (residues 7-208)== |
| - | <StructureSection load='3rle' size='340' side='right' caption='[[3rle]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='3rle' size='340' side='right'caption='[[3rle]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rle]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RLE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rle]] is a 1 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=3RLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RLE FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.649Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GORASP2, GOLPH6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3rle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rle RCSB], [http://www.ebi.ac.uk/pdbsum/3rle PDBsum]</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=3rle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rle OCA], [https://pdbe.org/3rle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rle RCSB], [https://www.ebi.ac.uk/pdbsum/3rle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rle ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3rle" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Foote, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Heroux, A]] | + | [[Category: Foote A]] |
| - | [[Category: Linstedt, A D]] | + | [[Category: Heroux A]] |
| - | [[Category: Macbeth, M R]] | + | [[Category: Linstedt AD]] |
| - | [[Category: Sengupta, D]] | + | [[Category: Macbeth MR]] |
| - | [[Category: Truschel, S T]] | + | [[Category: Sengupta D]] |
| - | [[Category: Golgi]]
| + | [[Category: Truschel ST]] |
| - | [[Category: Golgin]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Pdz]]
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| - | [[Category: Tether]]
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| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Biogenesis of the ribbon-like membrane network of the mammalian Golgi requires membrane tethering by the conserved GRASP domain in GRASP65 and GRASP55, yet the tethering mechanism is not fully understood. Here, we report the crystal structure of the GRASP55 GRASP domain, which revealed an unusual arrangement of two tandem PDZ folds that more closely resemble prokaryotic PDZ domains. Biochemical and functional data indicated that the interaction between the ligand-binding pocket of PDZ1 and an internal ligand on PDZ2 mediates the GRASP self-interaction, and structural analyses suggest that this occurs via a unique mode of internal PDZ ligand recognition. Our data uncover the structural basis for ligand specificity and provide insight into the mechanism of GRASP-dependent membrane tethering of analogous Golgi cisternae.
Structure of the Membrane-tethering GRASP Domain Reveals a Unique PDZ Ligand Interaction That Mediates Golgi Biogenesis.,Truschel ST, Sengupta D, Foote A, Heroux A, Macbeth MR, Linstedt AD J Biol Chem. 2011 Jun 10;286(23):20125-9. Epub 2011 Apr 22. PMID:21515684[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 1999 Sep 15;18(18):4949-60. PMID:10487747 doi:http://dx.doi.org/10.1093/emboj/18.18.4949
- ↑ Truschel ST, Sengupta D, Foote A, Heroux A, Macbeth MR, Linstedt AD. Structure of the Membrane-tethering GRASP Domain Reveals a Unique PDZ Ligand Interaction That Mediates Golgi Biogenesis. J Biol Chem. 2011 Jun 10;286(23):20125-9. Epub 2011 Apr 22. PMID:21515684 doi:10.1074/jbc.C111.245324
- ↑ Truschel ST, Sengupta D, Foote A, Heroux A, Macbeth MR, Linstedt AD. Structure of the Membrane-tethering GRASP Domain Reveals a Unique PDZ Ligand Interaction That Mediates Golgi Biogenesis. J Biol Chem. 2011 Jun 10;286(23):20125-9. Epub 2011 Apr 22. PMID:21515684 doi:10.1074/jbc.C111.245324
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