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| | <StructureSection load='1va7' size='340' side='right'caption='[[1va7]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1va7' size='340' side='right'caption='[[1va7]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1va7]] is a 4 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=1VA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1va7]] is a 4 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=1VA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ruw|1ruw]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1va7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va7 OCA], [https://pdbe.org/1va7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va7 RCSB], [https://www.ebi.ac.uk/pdbsum/1va7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va7 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=1va7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va7 OCA], [https://pdbe.org/1va7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va7 RCSB], [https://www.ebi.ac.uk/pdbsum/1va7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MYO3_YEAST MYO3_YEAST]] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.<ref>PMID:8682864</ref> <ref>PMID:8614799</ref> <ref>PMID:9388196</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref>
| + | [https://www.uniprot.org/uniprot/MYO3_YEAST MYO3_YEAST] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.<ref>PMID:8682864</ref> <ref>PMID:8614799</ref> <ref>PMID:9388196</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kursula, P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Lehmann, F]] | + | [[Category: Kursula P]] |
| - | [[Category: Song, Y H]] | + | [[Category: Lehmann F]] |
| - | [[Category: Wilmanns, M]] | + | [[Category: Song YH]] |
| - | [[Category: Contractile protein]]
| + | [[Category: Wilmanns M]] |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| Structural highlights
Function
MYO3_YEAST One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J Cell Biol. 1996 Jun;133(6):1277-91. PMID:8682864
- ↑ Geli MI, Riezman H. Role of type I myosins in receptor-mediated endocytosis in yeast. Science. 1996 Apr 26;272(5261):533-5. PMID:8614799
- ↑ Wu C, Lytvyn V, Thomas DY, Leberer E. The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast. J Biol Chem. 1997 Dec 5;272(49):30623-6. PMID:9388196
- ↑ Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, Leberer E, Whiteway M, Thomas DY, Boone C. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol. 2000 Jan 24;148(2):353-62. PMID:10648568
- ↑ Lechler T, Shevchenko A, Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol. 2000 Jan 24;148(2):363-73. PMID:10648569
- ↑ Wesche S, Arnold M, Jansen RP. The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function. Curr Biol. 2003 Apr 29;13(9):715-24. PMID:12725728
- ↑ Toi H, Fujimura-Kamada K, Irie K, Takai Y, Todo S, Tanaka K. She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae. Mol Biol Cell. 2003 Jun;14(6):2237-49. Epub 2003 Feb 6. PMID:12808026 doi:http://dx.doi.org/10.1091/mbc.E02-09-0616
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