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| | ==Structure of Dictyostelium Discoideum Myosin VII MyTH4-FERM MF2 domain== | | ==Structure of Dictyostelium Discoideum Myosin VII MyTH4-FERM MF2 domain== |
| - | <StructureSection load='5ejr' size='340' side='right' caption='[[5ejr]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5ejr' size='340' side='right'caption='[[5ejr]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ejr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EJR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EJR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ejr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EJR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">myoI, DDB_G0274455 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5ejr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ejr OCA], [http://pdbe.org/5ejr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ejr RCSB], [http://www.ebi.ac.uk/pdbsum/5ejr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ejr 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=5ejr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ejr OCA], [https://pdbe.org/5ejr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ejr RCSB], [https://www.ebi.ac.uk/pdbsum/5ejr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ejr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYOI_DICDI MYOI_DICDI]] Myosins are actin-based motor molecules with ATPase activity. Involved in the early steps of phagocytosis and adhesion.<ref>PMID:10574761</ref> <ref>PMID:11267868</ref> <ref>PMID:15826949</ref> | + | [https://www.uniprot.org/uniprot/MYOI_DICDI MYOI_DICDI] Myosins are actin-based motor molecules with ATPase activity. Involved in the early steps of phagocytosis and adhesion.<ref>PMID:10574761</ref> <ref>PMID:11267868</ref> <ref>PMID:15826949</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5ejr" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ejr" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 11735]] | + | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Clause, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Houdusse, A]] | + | [[Category: Clause J]] |
| - | [[Category: Planelles-Herrero, V J]] | + | [[Category: Houdusse A]] |
| - | [[Category: Sirkia, H]] | + | [[Category: Planelles-Herrero VJ]] |
| - | [[Category: Sourigues, Y]] | + | [[Category: Sirkia H]] |
| - | [[Category: Titus, M A]] | + | [[Category: Sourigues Y]] |
| - | [[Category: Motor myosin]]
| + | [[Category: Titus MA]] |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Myosin]]
| + | |
| - | [[Category: Myosin tail]]
| + | |
| - | [[Category: Myth4-ferm]]
| + | |
| Structural highlights
Function
MYOI_DICDI Myosins are actin-based motor molecules with ATPase activity. Involved in the early steps of phagocytosis and adhesion.[1] [2] [3]
Publication Abstract from PubMed
Myosins containing MyTH4-FERM (myosin tail homology 4-band 4.1, ezrin, radixin, moesin, or MF) domains in their tails are found in a wide range of phylogenetically divergent organisms, such as humans and the social amoeba Dictyostelium (Dd). Interestingly, evolutionarily distant MF myosins have similar roles in the extension of actin-filled membrane protrusions such as filopodia and bind to microtubules (MT), suggesting that the core functions of these MF myosins have been highly conserved over evolution. The structures of two DdMyo7 signature MF domains have been determined and comparison with mammalian MF structures reveals that characteristic features of MF domains are conserved. However, across millions of years of evolution conserved class-specific insertions are seen to alter the surfaces and the orientation of subdomains with respect to each other, likely resulting in new sites for binding partners. The MyTH4 domains of Myo10 and DdMyo7 bind to MT with micromolar affinity but, surprisingly, their MT binding sites are on opposite surfaces of the MyTH4 domain. The structural analysis in combination with comparison of diverse MF myosin sequences provides evidence that myosin tail domain features can be maintained without strict conservation of motifs. The results illustrate how tuning of existing features can give rise to new structures while preserving the general properties necessary for myosin tails. Thus, tinkering with the MF domain enables it to serve as a multifunctional platform for cooperative recruitment of various partners, allowing common properties such as autoinhibition of the motor and microtubule binding to arise through convergent evolution.
Myosin MyTH4-FERM structures highlight important principles of convergent evolution.,Planelles-Herrero VJ, Blanc F, Sirigu S, Sirkia H, Clause J, Sourigues Y, Johnsrud DO, Amigues B, Cecchini M, Gilbert SP, Houdusse A, Titus MA Proc Natl Acad Sci U S A. 2016 May 24;113(21):E2906-15. doi:, 10.1073/pnas.1600736113. Epub 2016 May 10. PMID:27166421[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Titus MA. A class VII unconventional myosin is required for phagocytosis. Curr Biol. 1999 Nov 18;9(22):1297-303. PMID:10574761
- ↑ Tuxworth RI, Weber I, Wessels D, Addicks GC, Soll DR, Gerisch G, Titus MA. A role for myosin VII in dynamic cell adhesion. Curr Biol. 2001 Mar 6;11(5):318-29. PMID:11267868
- ↑ Tuxworth RI, Stephens S, Ryan ZC, Titus MA. Identification of a myosin VII-talin complex. J Biol Chem. 2005 Jul 15;280(28):26557-64. Epub 2005 Apr 11. PMID:15826949 doi:http://dx.doi.org/M503699200
- ↑ Planelles-Herrero VJ, Blanc F, Sirigu S, Sirkia H, Clause J, Sourigues Y, Johnsrud DO, Amigues B, Cecchini M, Gilbert SP, Houdusse A, Titus MA. Myosin MyTH4-FERM structures highlight important principles of convergent evolution. Proc Natl Acad Sci U S A. 2016 May 24;113(21):E2906-15. doi:, 10.1073/pnas.1600736113. Epub 2016 May 10. PMID:27166421 doi:http://dx.doi.org/10.1073/pnas.1600736113
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