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| | ==Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil== | | ==Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil== |
| - | <StructureSection load='2n9b' size='340' side='right' caption='[[2n9b]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2n9b' size='340' side='right'caption='[[2n9b]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n9b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N9B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n9b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9B FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lw9|2lw9]], [[2zta|2zta]]</td></tr> | + | </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=2n9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9b OCA], [https://pdbe.org/2n9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9b RCSB], [https://www.ebi.ac.uk/pdbsum/2n9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9b ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GCN4 AAS3 ARG9 YEL009C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=2n9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9b OCA], [http://pdbe.org/2n9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n9b RCSB], [http://www.ebi.ac.uk/pdbsum/2n9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYO10_BOVIN MYO10_BOVIN]] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.<ref>PMID:11457842</ref> <ref>PMID:15156152</ref> <ref>PMID:15705568</ref> <ref>PMID:16894163</ref> <ref>PMID:20081229</ref> <ref>PMID:20364131</ref> <ref>PMID:20392702</ref> <ref>PMID:20930142</ref> <ref>PMID:21666676</ref> | + | [https://www.uniprot.org/uniprot/MYO10_BOVIN MYO10_BOVIN] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.<ref>PMID:11457842</ref> <ref>PMID:15156152</ref> <ref>PMID:15705568</ref> <ref>PMID:16894163</ref> <ref>PMID:20081229</ref> <ref>PMID:20364131</ref> <ref>PMID:20392702</ref> <ref>PMID:20930142</ref> <ref>PMID:21666676</ref> [https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Coiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability. |
| | + | |
| | + | Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.,Vavra KC, Xia Y, Rock RS Biophys J. 2016 Jun 7;110(11):2517-2527. doi: 10.1016/j.bpj.2016.04.048. PMID:27276269<ref>PMID:27276269</ref> |
| | + | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 2n9b" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Rock, R S]] | + | [[Category: Large Structures]] |
| - | [[Category: Vavra, K C]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Xia, Y]] | + | [[Category: Rock RS]] |
| - | [[Category: Anti-parallel coiled-coil]] | + | [[Category: Vavra KC]] |
| - | [[Category: Coiled-coil]] | + | [[Category: Xia Y]] |
| - | [[Category: Motor protein-transcription complex]]
| + | |
| Structural highlights
Function
MYO10_BOVIN In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.[1] [2] [3] [4] [5] [6] [7] [8] [9] GCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
Publication Abstract from PubMed
Coiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability.
Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.,Vavra KC, Xia Y, Rock RS Biophys J. 2016 Jun 7;110(11):2517-2527. doi: 10.1016/j.bpj.2016.04.048. PMID:27276269[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Homma K, Saito J, Ikebe R, Ikebe M. Motor function and regulation of myosin X. J Biol Chem. 2001 Sep 7;276(36):34348-54. Epub 2001 Jul 16. PMID:11457842 doi:http://dx.doi.org/10.1074/jbc.M104785200
- ↑ Zhang H, Berg JS, Li Z, Wang Y, Lang P, Sousa AD, Bhaskar A, Cheney RE, Stromblad S. Myosin-X provides a motor-based link between integrins and the cytoskeleton. Nat Cell Biol. 2004 Jun;6(6):523-31. Epub 2004 May 23. PMID:15156152 doi:http://dx.doi.org/10.1038/ncb1136
- ↑ Kovacs M, Wang F, Sellers JR. Mechanism of action of myosin X, a membrane-associated molecular motor. J Biol Chem. 2005 Apr 15;280(15):15071-83. Epub 2005 Feb 10. PMID:15705568 doi:http://dx.doi.org/10.1074/jbc.M500616200
- ↑ Bohil AB, Robertson BW, Cheney RE. Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12411-6. Epub 2006 Aug 7. PMID:16894163 doi:10.1073/pnas.0602443103
- ↑ McMichael BK, Cheney RE, Lee BS. Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules. J Biol Chem. 2010 Mar 26;285(13):9506-15. doi: 10.1074/jbc.M109.017269. Epub 2010, Jan 17. PMID:20081229 doi:http://dx.doi.org/10.1074/jbc.M109.017269
- ↑ Sun Y, Sato O, Ruhnow F, Arsenault ME, Ikebe M, Goldman YE. Single-molecule stepping and structural dynamics of myosin X. Nat Struct Mol Biol. 2010 Apr;17(4):485-91. doi: 10.1038/nsmb.1785. Epub 2010 Apr, 4. PMID:20364131 doi:http://dx.doi.org/10.1038/nsmb.1785
- ↑ Watanabe TM, Tokuo H, Gonda K, Higuchi H, Ikebe M. Myosin-X induces filopodia by multiple elongation mechanism. J Biol Chem. 2010 Jun 18;285(25):19605-14. doi: 10.1074/jbc.M109.093864. Epub, 2010 Apr 13. PMID:20392702 doi:http://dx.doi.org/10.1074/jbc.M109.093864
- ↑ Plantard L, Arjonen A, Lock JG, Nurani G, Ivaska J, Stromblad S. PtdIns(3,4,5)P(3) is a regulator of myosin-X localization and filopodia formation. J Cell Sci. 2010 Oct 15;123(Pt 20):3525-34. doi: 10.1242/jcs.069609. PMID:20930142 doi:http://dx.doi.org/10.1242/jcs.069609
- ↑ Umeki N, Jung HS, Sakai T, Sato O, Ikebe R, Ikebe M. Phospholipid-dependent regulation of the motor activity of myosin X. Nat Struct Mol Biol. 2011 Jun 12;18(7):783-8. doi: 10.1038/nsmb.2065. PMID:21666676 doi:http://dx.doi.org/10.1038/nsmb.2065
- ↑ Vavra KC, Xia Y, Rock RS. Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection. Biophys J. 2016 Jun 7;110(11):2517-2527. doi: 10.1016/j.bpj.2016.04.048. PMID:27276269 doi:http://dx.doi.org/10.1016/j.bpj.2016.04.048
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