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< | ==MYOSIN DIGESTED BY PAPAIN== | ||
<StructureSection load='1b7t' size='340' side='right'caption='[[1b7t]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
You may | == Structural highlights == | ||
or the | <table><tr><td colspan='2'>[[1b7t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. The June 2001 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Myosin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2001_6 10.2210/rcsb_pdb/mom_2001_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B7T 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]] 2.5Å</td></tr> | |||
<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></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=1b7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7t OCA], [https://pdbe.org/1b7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b7t RCSB], [https://www.ebi.ac.uk/pdbsum/1b7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b7t ProSAT]</span></td></tr> | |||
</table> | |||
== 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/1b7t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1b7t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre-power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible "joints" produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis ("ATP") states of the contractile cycle in which the myosin heads stay detached from actin. | |||
Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.,Houdusse A, Kalabokis VN, Himmel D, Szent-Gyorgyi AG, Cohen C Cell. 1999 May 14;97(4):459-70. PMID:10338210<ref>PMID:10338210</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1b7t" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myosin 3D Structures|Myosin 3D Structures]] | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Argopecten irradians]] | [[Category: Argopecten irradians]] | ||
[[Category: Large Structures]] | |||
[[Category: Myosin]] | [[Category: Myosin]] | ||
[[Category: | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Cohen | [[Category: Cohen C]] | ||
[[Category: Himmel | [[Category: Himmel D]] | ||
[[Category: Houdusse | [[Category: Houdusse A]] | ||
[[Category: Kalabokis | [[Category: Kalabokis V]] | ||
[[Category: Szent-Gyorgyi | [[Category: Szent-Gyorgyi AG]] | ||
Latest revision as of 17:49, 20 September 2023
MYOSIN DIGESTED BY PAPAINMYOSIN DIGESTED BY PAPAIN
Structural highlights
FunctionMYS_ARGIR Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre-power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible "joints" produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis ("ATP") states of the contractile cycle in which the myosin heads stay detached from actin. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.,Houdusse A, Kalabokis VN, Himmel D, Szent-Gyorgyi AG, Cohen C Cell. 1999 May 14;97(4):459-70. PMID:10338210[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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