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<StructureSection load='1scm' size='340' side='right'caption='[[1scm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1scm' size='340' side='right'caption='[[1scm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1scm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Argir Argir]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1scm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCM 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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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></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=1scm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scm OCA], [https://pdbe.org/1scm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scm RCSB], [https://www.ebi.ac.uk/pdbsum/1scm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scm 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=1scm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scm OCA], [https://pdbe.org/1scm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scm RCSB], [https://www.ebi.ac.uk/pdbsum/1scm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR]] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [[https://www.uniprot.org/uniprot/MLE_ARGIR MLE_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [[https://www.uniprot.org/uniprot/MLR_ARGIR MLR_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.  
[https://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1scm ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1scm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.
Structure of the regulatory domain of scallop myosin at 2.8 A resolution.,Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Gyorgyi AG, Cohen C Nature. 1994 Mar 24;368(6469):306-12. PMID:8127365<ref>PMID:8127365</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1scm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myosin 3D Structures|Myosin 3D Structures]]
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Argir]]
[[Category: Argopecten irradians]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cohen, C]]
[[Category: Cohen C]]
[[Category: Xie, X]]
[[Category: Xie X]]
[[Category: Calcium-binding protein]]
Retrieved from "https://proteopedia.org/1scm"