5ejr: Difference between revisions
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==Structure of Dictyostelium Discoideum Myosin VII MyTH4-FERM MF2 domain== | |||
<StructureSection load='5ejr' size='340' side='right' caption='[[5ejr]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ejr]] is a 1 chain structure. 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> | |||
</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> | |||
<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> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27166421</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Planelles-Herrero, V | <div class="pdbe-citations 5ejr" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clause, J]] | |||
[[Category: Houdusse, A]] | |||
[[Category: Planelles-Herrero, V J]] | |||
[[Category: Sirkia, H]] | [[Category: Sirkia, H]] | ||
[[Category: Sourigues, Y]] | [[Category: Sourigues, Y]] | ||
[[Category: | [[Category: Titus, M A]] | ||
[[Category: | [[Category: Motor myosin]] | ||
[[Category: | [[Category: Motor protein]] | ||
[[Category: Myosin]] | |||
[[Category: Myosin tail]] | |||
[[Category: Myth4-ferm]] | |||
Revision as of 05:18, 13 July 2016
Structure of Dictyostelium Discoideum Myosin VII MyTH4-FERM MF2 domainStructure of Dictyostelium Discoideum Myosin VII MyTH4-FERM MF2 domain
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 PubMedMyosins 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. References
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