1sr6

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[[Image:1sr6.gif|left|200px]]
 
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{{Structure
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==Structure of nucleotide-free scallop myosin S1==
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|PDB= 1sr6 |SIZE=350|CAPTION= <scene name='initialview01'>1sr6</scene>, resolution 2.75&Aring;
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<StructureSection load='1sr6' size='340' side='right'caption='[[1sr6]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1sr6]] 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=1SR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SR6 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.75&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1sr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr6 OCA], [https://pdbe.org/1sr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1sr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sr6 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1s5g|1S5G]], [[1qvi|1QVI]], [[1kk8|1KK8]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr6 OCA], [http://www.ebi.ac.uk/pdbsum/1sr6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sr6 RCSB]</span>
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== Function ==
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}}
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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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1sr6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1sr6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near-rigor state (lever arm =45 degrees to the helical actin axis) shows the diphosphate moiety positioned on the surface of the nucleotide-binding pocket, rather than deep within it as had been observed previously. This conformation strongly suggests a specific mode of entry and exit of the nucleotide from the nucleotide-binding pocket through the so-called "front door." In addition, using a variety of scallop structures, including a relatively high-resolution 2.75-A nucleotide-free near-rigor structure, we have identified a conserved complex salt bridge connecting the 50-kDa upper and N-terminal subdomains. This salt bridge is present only in crystal structures of muscle myosin isoforms that exhibit a strong reciprocal relationship (also known as coupling) between actin and nucleotide affinity.
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'''Structure of nucleotide-free scallop myosin S1'''
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Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding.,Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:15184651<ref>PMID:15184651</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1sr6" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near-rigor state (lever arm =45 degrees to the helical actin axis) shows the diphosphate moiety positioned on the surface of the nucleotide-binding pocket, rather than deep within it as had been observed previously. This conformation strongly suggests a specific mode of entry and exit of the nucleotide from the nucleotide-binding pocket through the so-called "front door." In addition, using a variety of scallop structures, including a relatively high-resolution 2.75-A nucleotide-free near-rigor structure, we have identified a conserved complex salt bridge connecting the 50-kDa upper and N-terminal subdomains. This salt bridge is present only in crystal structures of muscle myosin isoforms that exhibit a strong reciprocal relationship (also known as coupling) between actin and nucleotide affinity.
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*[[Myosin 3D Structures|Myosin 3D Structures]]
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== References ==
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==About this Structure==
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<references/>
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1SR6 is a [[Protein complex]] structure of sequences 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=1SR6 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding., Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15184651 15184651]
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[[Category: Argopecten irradians]]
[[Category: Argopecten irradians]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Cohen, C.]]
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[[Category: Cohen C]]
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[[Category: Gourinath, S.]]
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[[Category: Gourinath S]]
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[[Category: Himmel, D M.]]
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[[Category: Himmel DM]]
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[[Category: Risal, D.]]
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[[Category: Risal D]]
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[[Category: Szent-Gyorgyi, A G.]]
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[[Category: Szent-Gyorgyi AG]]
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[[Category: complex salt bridge]]
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[[Category: near rigor]]
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[[Category: novel conformation of nucleotide]]
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[[Category: scallop myosin s1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:54 2008''
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Current revision

Structure of nucleotide-free scallop myosin S1

PDB ID 1sr6

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