1dfk: Difference between revisions

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[[Image:1dfk.jpg|left|200px]]


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==NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE==
The line below this paragraph, containing "STRUCTURE_1dfk", creates the "Structure Box" on the page.
<StructureSection load='1dfk' size='340' side='right'caption='[[1dfk]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dfk]] 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=1DFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFK FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2&#8491;</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=CA:CALCIUM+ION'>CA</scene></td></tr>
{{STRUCTURE_1dfk| PDB=1dfk |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfk OCA], [https://pdbe.org/1dfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfk RCSB], [https://www.ebi.ac.uk/pdbsum/1dfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfk 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/df/1dfk_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=1dfk ConSurf].
<div style="clear:both"></div>


'''NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE'''
==See Also==
 
*[[Myosin 3D Structures|Myosin 3D Structures]]
 
__TOC__
==Overview==
</StructureSection>
We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free state and in the presence of MgADP.V04, corresponding to the transition state. These two new structures, together with the previously determined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reveal three conformations of an intact S1 obtained from a single isoform. These studies, together with new crystallization results, show how the conformation of the motor depends on the nucleotide content of the active site. The resolution of the two new structures ( approximately 4 A) is sufficient to establish the relative positions of the subdomains and the overall conformation of the joints within the motor domain as well as the position of the lever arm. Comparison of available crystal structures from different myosin isoforms and truncated constructs in either the nucleotide-free or transition states indicates that the major features within the motor domain are relatively invariant in both these states. In contrast, the position of the lever arm varies significantly between different isoforms. These results indicate that the heavy-chain helix is pliant at the junction between the converter and the lever arm and that factors other than the precise position of the converter can influence the position of the lever arm. It is possible that this pliant junction in the myosin head contributes to the compliance known to be present in the crossbridge.
 
==About this Structure==
1DFK 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=1DFK OCA].
 
==Reference==
Three conformational states of scallop myosin S1., Houdusse A, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11238-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11016966 11016966]
[[Category: Argopecten irradians]]
[[Category: Argopecten irradians]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Cohen, C.]]
[[Category: Cohen C]]
[[Category: Houdusse, A.]]
[[Category: Houdusse A]]
[[Category: Szent-Gyorgyi, A G.]]
[[Category: Szent-Gyorgyi AG]]
[[Category: Conformational change]]
[[Category: Myosin motor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:47:58 2008''

Latest revision as of 09:53, 7 February 2024

NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATENUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE

Structural highlights

1dfk is a 3 chain structure with sequence from Argopecten irradians. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1dfk, resolution 4.20Å

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