1lkx

<table><tr><td colspan='2'>[[1lkx]] is a 4 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=1LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LKX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=1lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lkx OCA], [http://pdbe.org/1lkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lkx RCSB], [http://www.ebi.ac.uk/pdbsum/1lkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lkx ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MYOE_DICDI MYOE_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. May play a role in moving membranes relative to actin.

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== Publication Abstract from PubMed ==

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently resolved molecules, highlighting regions that undergo large conformational changes. Differences are particularly pronounced in the actin binding region and the converter domain. The changes in position of the converter domain reflect movements both parallel to and perpendicular to the actin axis. The orientation of the converter domain is approximately 30 degrees further up than in other myosin structures, indicating that MyoE can produce a larger power stroke by rotating its lever arm through a larger angle. The role of extended loops near the actin-binding site is discussed in the context of cellular localization. The core regions of the motor domain are similar, and the structure reveals how that core is stabilized in the absence of an N-terminal SH3-like domain.

Crystal structure of the motor domain of a class-I myosin.,Kollmar M, Durrwang U, Kliche W, Manstein DJ, Kull FJ EMBO J. 2002 Jun 3;21(11):2517-25. PMID:12032065<ref>PMID:12032065</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lkx" style="background-color:#fffaf0;"></div>

*[[Myosin|Myosin]]

[[Category: Atcc 11735]]

[[Category: Durrwang, U]]

[[Category: Kliche, W]]

[[Category: Kollmar, M]]

[[Category: Kull, F J]]

[[Category: Manstein, D J]]

[[Category: Myosin motor domain]]