1dfl: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1dfl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfl, resolution 4.20Å" /> '''SCALLOP MYOSIN S1 CO...
 
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1dfl.jpg|left|200px]]<br /><applet load="1dfl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dfl, resolution 4.20&Aring;" />
'''SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE'''<br />


==Overview==
==SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE==
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.
<StructureSection load='1dfl' size='340' side='right'caption='[[1dfl]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dfl]] is a 6 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=1DFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFL 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]] 4.2&#8491;</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>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=1dfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfl OCA], [https://pdbe.org/1dfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfl RCSB], [https://www.ebi.ac.uk/pdbsum/1dfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfl 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/1dfl_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=1dfl ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DFL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with CA, MG, VO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DFL OCA].
*[[Myosin 3D Structures|Myosin 3D Structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: ADP]]
[[Category: CA]]
[[Category: MG]]
[[Category: VO4]]
[[Category: conformational changes]]
[[Category: contractile protein]]
[[Category: myosin motor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:14:59 2007''

Latest revision as of 09:53, 7 February 2024

SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATESCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE

Structural highlights

1dfl is a 6 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

1dfl, resolution 4.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA