View source for 3mjx


==Crystal structure of myosin-2 motor domain in complex with ADP-Metavanadate and blebbistatin==
<StructureSection load='3mjx' size='340' side='right'caption='[[3mjx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mjx]] 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=3MJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MJX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AD9:ADP+METAVANADATE'>AD9</scene>, <scene name='pdbligand=BIT:(-)-1-PHENYL-1,2,3,4-TETRAHYDRO-4-HYDROXYPYRROLO[2,3-B]-7-METHYLQUINOLIN-4-ONE'>BIT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3mjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mjx OCA], [https://pdbe.org/3mjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mjx RCSB], [https://www.ebi.ac.uk/pdbsum/3mjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mjx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have identified pentabromopseudilin (PBP) as a potent inhibitor of myosin-dependent processes such as isometric tension development and unloaded shortening velocity. PBP-induced reductions in the rate constants for ATP binding, ATP hydrolysis and ADP dissociation extend the time required per myosin ATPase cycle in the absence and presence of actin. Additionally, coupling between the actin and nucleotide binding sites is reduced in the presence of the inhibitor. The selectivity of PBP differs from that observed with other myosin inhibitors. To elucidate the binding mode of PBP, we crystallized the Dictyostelium myosin-2 motor domain in the presence of Mg(2+)-ADP-meta-vanadate and PBP. The electron density for PBP is unambiguous and shows PBP to bind at a previously unknown allosteric site near the tip of the 50-kDa domain, at a distance of 16 A from the nucleotide binding site and 7.5 A away from the blebbistatin binding pocket.

The mechanism of pentabromopseudilin inhibition of myosin motor activity.,Fedorov R, Bohl M, Tsiavaliaris G, Hartmann FK, Taft MH, Baruch P, Brenner B, Martin R, Knolker HJ, Gutzeit HO, Manstein DJ Nat Struct Mol Biol. 2009 Jan;16(1):80-8. Epub 2009 Jan 4. PMID:19122661<ref>PMID:19122661</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mjx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Baruch P]]
[[Category: Bauer S]]
[[Category: Fedorov R]]
[[Category: Manstein DJ]]