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1qvi

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==Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head==
==Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head==
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<StructureSection load='1qvi' size='340' side='right' caption='[[1qvi]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
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<StructureSection load='1qvi' size='340' side='right'caption='[[1qvi]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qvi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QVI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qvi]] 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=1QVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QVI FirstGlance]. <br>
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</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b7t|1b7t]], [[1dfl|1dfl]], [[1kk7|1kk7]], [[1kk8|1kk8]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
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<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=1qvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qvi OCA], [http://pdbe.org/1qvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qvi RCSB], [http://www.ebi.ac.uk/pdbsum/1qvi PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qvi OCA], [https://pdbe.org/1qvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qvi RCSB], [https://www.ebi.ac.uk/pdbsum/1qvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qvi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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. [[http://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. [[http://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.
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qvi_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qvi_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
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*[[Myosin|Myosin]]
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*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Argopecten irradians]]
[[Category: Argopecten irradians]]
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[[Category: Brown, J H]]
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[[Category: Large Structures]]
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[[Category: Cohen, C]]
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[[Category: Brown JH]]
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[[Category: Gourinath, S]]
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[[Category: Cohen C]]
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[[Category: Himmel, D M]]
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[[Category: Gourinath S]]
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[[Category: Reshetnikova, L]]
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[[Category: Himmel DM]]
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[[Category: Szent-Gyrgyi, A G]]
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[[Category: Reshetnikova L]]
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[[Category: Contractile protein]]
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[[Category: Szent-Gyrgyi AG]]
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[[Category: Internally-uncoupled state]]
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[[Category: Pliant region]]
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[[Category: Pre-power stroke state]]
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[[Category: Sh1 helix]]
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Current revision

Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head

PDB ID 1qvi

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