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| | <StructureSection load='2x51' size='340' side='right'caption='[[2x51]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2x51' size='340' side='right'caption='[[2x51]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X51 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X51 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome] and [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X51 FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v26|2v26]], [[2vas|2vas]], [[2bbm|2bbm]], [[4cln|4cln]], [[1mxe|1mxe]], [[2bkh|2bkh]], [[2vb6|2vb6]], [[2bki|2bki]], [[2bbn|2bbn]], [[3l9i|3l9i]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v26|2v26]], [[2vas|2vas]], [[2bbm|2bbm]], [[4cln|4cln]], [[1mxe|1mxe]], [[2bkh|2bkh]], [[2vb6|2vb6]], [[2bki|2bki]], [[2bbn|2bbn]], [[3l9i|3l9i]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x51 OCA], [http://pdbe.org/2x51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x51 RCSB], [http://www.ebi.ac.uk/pdbsum/2x51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x51 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=2x51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x51 OCA], [https://pdbe.org/2x51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x51 RCSB], [https://www.ebi.ac.uk/pdbsum/2x51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x51 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYO6_PIG MYO6_PIG]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).<ref>PMID:16917816</ref> [[http://www.uniprot.org/uniprot/CALM_DROME CALM_DROME]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | + | [[https://www.uniprot.org/uniprot/MYO6_PIG MYO6_PIG]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).<ref>PMID:16917816</ref> [[https://www.uniprot.org/uniprot/CALM_DROME CALM_DROME]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
Function
[MYO6_PIG] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).[1] [CALM_DROME] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Publication Abstract from PubMed
Myosin VI is unique in its directionality among myosin superfamily members and also displays a slow and strain-dependent rate of ATP binding that allows for gating between its heads. In this study we demonstrate that leucine 310 is positioned by a class VI-specific insert, insert-1, so as to account for the selective hindrance of ATP versus ADP binding. Mutation of leucine 310 to glycine removes all influence of insert-1 on ATP binding. Furthermore, by analyzing myosin VI structures with either leucine 310 substituted to a glycine or complete removal of insert-1, we conclude that nucleotides may initially bind to myosin by their purine rings before docking their phosphate moieties. Otherwise, insert-1 could not exert a differential influence on ATP versus ADP binding.
Role of Insert-1 of Myosin VI in Modulating Nucleotide Affinity.,Pylypenko O, Song L, Squires G, Liu X, Zong AB, Houdusse A, Sweeney HL J Biol Chem. 2011 Apr 1;286(13):11716-23. Epub 2011 Jan 29. PMID:21278381[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Naccache SN, Hasson T. Myosin VI altered at threonine 406 stabilizes actin filaments in vivo. Cell Motil Cytoskeleton. 2006 Oct;63(10):633-45. PMID:16917816 doi:http://dx.doi.org/10.1002/cm.20150
- ↑ Pylypenko O, Song L, Squires G, Liu X, Zong AB, Houdusse A, Sweeney HL. Role of Insert-1 of Myosin VI in Modulating Nucleotide Affinity. J Biol Chem. 2011 Apr 1;286(13):11716-23. Epub 2011 Jan 29. PMID:21278381 doi:10.1074/jbc.M110.200626
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