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| | <StructureSection load='3a58' size='340' side='right'caption='[[3a58]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3a58' size='340' side='right'caption='[[3a58]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a58]] is a 6 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=3A58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A58 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a58]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A58 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.6Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC3, PSL1, YER008C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), RHO1, YPR165W, P9325.3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3a58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a58 OCA], [https://pdbe.org/3a58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a58 RCSB], [https://www.ebi.ac.uk/pdbsum/3a58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a58 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=3a58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a58 OCA], [https://pdbe.org/3a58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a58 RCSB], [https://www.ebi.ac.uk/pdbsum/3a58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a58 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SEC3_YEAST SEC3_YEAST]] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [[https://www.uniprot.org/uniprot/RHO1_YEAST RHO1_YEAST]] Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7.<ref>PMID:8195291</ref> <ref>PMID:7579704</ref> <ref>PMID:8846785</ref> <ref>PMID:8947028</ref> <ref>PMID:8621575</ref> <ref>PMID:8602514</ref> <ref>PMID:8602515</ref> <ref>PMID:11283608</ref> <ref>PMID:11447600</ref> <ref>PMID:12419188</ref> <ref>PMID:12207708</ref> <ref>PMID:12810699</ref> <ref>PMID:12928491</ref> <ref>PMID:15514049</ref> <ref>PMID:15596542</ref>
| + | [https://www.uniprot.org/uniprot/SEC3_YEAST SEC3_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/3a58_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/3a58_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fukai, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mimura, H]] | + | [[Category: Fukai S]] |
| - | [[Category: Sato, Y]] | + | [[Category: Mimura H]] |
| - | [[Category: Yamagata, A]] | + | [[Category: Sato Y]] |
| - | [[Category: Yamashita, M]] | + | [[Category: Yamagata A]] |
| - | [[Category: Yoshikawa, A]] | + | [[Category: Yamashita M]] |
| - | [[Category: Cell membrane]]
| + | [[Category: Yoshikawa A]] |
| - | [[Category: Endosome]]
| + | |
| - | [[Category: Exocytosis]]
| + | |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane traffic]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| - | [[Category: Ph domain]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Prenylation]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Protein transport-exocytosis complex]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
SEC3_YEAST Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The exocyst complex is a hetero-octameric protein complex that functions during cell polarization by tethering the secretory vesicle to the target membrane. The yeast exocyst subunit Sec3 binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) and the small GTPases Rho1 and Cdc42 via its N-terminal domain (Sec3-N), and these interactions target Sec3 to the plasma membrane. Here we report the crystal structure of the Sec3-N in complex with Rho1 at 2.6-A resolution. Sec3-N adopts a pleckstrin homology (PH) fold, despite having no detectable sequence homology with other PH domains of known structure. Clusters of conserved basic residues constitute a positively charged cleft, which was identified as a binding site for PtdIns(4,5)P(2). Residues Phe77, Ile115 and Leu131 of Sec3 bind to an extended hydrophobic surface formed around switch regions I and II of Rho1. To our knowledge, these are the first structural insights into how an exocyst subunit might interact with both protein and phospholipid factors on the target membrane.
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3.,Yamashita M, Kurokawa K, Sato Y, Yamagata A, Mimura H, Yoshikawa A, Sato K, Nakano A, Fukai S Nat Struct Mol Biol. 2010 Feb;17(2):180-6. Epub 2010 Jan 10. PMID:20062059[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamashita M, Kurokawa K, Sato Y, Yamagata A, Mimura H, Yoshikawa A, Sato K, Nakano A, Fukai S. Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3. Nat Struct Mol Biol. 2010 Feb;17(2):180-6. Epub 2010 Jan 10. PMID:20062059 doi:10.1038/nsmb.1722
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