2x51: Difference between revisions
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[[ | ==M6 DELTA INSERT1== | ||
<StructureSection load='2x51' size='340' side='right' caption='[[2x51]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X51 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x51 RCSB], [http://www.ebi.ac.uk/pdbsum/2x51 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21278381</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Calmodulin|Calmodulin]] | *[[Calmodulin|Calmodulin]] | ||
*[[Myosin|Myosin]] | *[[Myosin|Myosin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
Revision as of 04:01, 2 October 2014
M6 DELTA INSERT1M6 DELTA INSERT1
Structural highlights
Publication Abstract from PubMedMyosin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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