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| | <StructureSection load='5h3j' size='340' side='right'caption='[[5h3j]], [[Resolution|resolution]] 1.33Å' scene=''> | | <StructureSection load='5h3j' size='340' side='right'caption='[[5h3j]], [[Resolution|resolution]] 1.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h3j]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H3J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h3j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.33Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3j OCA], [http://pdbe.org/5h3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3j RCSB], [http://www.ebi.ac.uk/pdbsum/5h3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3j ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5h3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3j OCA], [https://pdbe.org/5h3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3j RCSB], [https://www.ebi.ac.uk/pdbsum/5h3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GORS2_MOUSE GORS2_MOUSE]] Plays a role in 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> [[http://www.uniprot.org/uniprot/GO45_MOUSE GO45_MOUSE]] Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface. | + | [https://www.uniprot.org/uniprot/GORS2_MOUSE GORS2_MOUSE] Plays a role in 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, B]] | + | [[Category: Mus musculus]] |
| - | [[Category: Shi, N]] | + | [[Category: Li B]] |
| - | [[Category: Zhao, J]] | + | [[Category: Shi N]] |
| - | [[Category: Golgi peripheral membrane protein]] | + | [[Category: Zhao J]] |
| - | [[Category: Golgin]]
| + | |
| - | [[Category: Pdz domain]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Tethering protein]]
| + | |
| Structural highlights
Function
GORS2_MOUSE Plays a role in 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]
Publication Abstract from PubMed
Golgin45 is required for normal Golgi structure and the transportation of protein from the ER. It forms a specific complex with GRASP55 in vivo Little is known regarding the molecular details of this interaction and its structural role in stacking of the Golgi complex. Here, we present the crystal structure of the GRASP domains of GRASP55 in complex with the Golgin45 C-terminal peptide, determined at 1.33 A resolution. Similar to the structure of GRASP65 bound to GM130 reported recently, this structure reveals more than one interacting site and involves both PDZ1 and PDZ2 domains of the GRASP simultaneously. The C-terminal peptides of Golgin45 and GM130 present a conserved PDZ domain binding motif sequence and recognize the canonical PDZ-peptide binding groove of the PDZ1 domains of GRASP55 and GRASP65. A main difference in this recognition process resides in a structural rearrangement of GRASP65-GM130 that does not occur for the GRASP55-Golgin45 complex. The binding site at the cleft between the PDZ1 and PDZ2 domains of GRASP65 is dominated by hydrophobic interactions with GM130 that are not observed in the GRASP55-Golgin45 complex. In addition, a unique zinc finger structure is revealed in the GRASP55-Golgin45 complex crystal structure. Mutagenesis experiments support these structural observations and demonstrate that two of these sites are required to form a stable complex. Finally, a novel Golgi stacking model is proposed according to these structural findings.
Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.,Zhao J, Li B, Huang X, Morelli X, Shi N J Biol Chem. 2017 Feb 17;292(7):2956-2965. doi: 10.1074/jbc.M116.765990. Epub, 2017 Jan 3. PMID:28049725[2]
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
- ↑ Zhao J, Li B, Huang X, Morelli X, Shi N. Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45. J Biol Chem. 2017 Feb 17;292(7):2956-2965. doi: 10.1074/jbc.M116.765990. Epub, 2017 Jan 3. PMID:28049725 doi:http://dx.doi.org/10.1074/jbc.M116.765990
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