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1dfk

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Revision as of 04:13, 11 September 2015

NUCLEOTIDE-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.
Ligands:
Related:	1b7t, 1dfl
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MYS_ARGIR] Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [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. [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.

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 PubMed

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.

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:11016966^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Houdusse A, Szent-Gyorgyi AG, Cohen C. Three conformational states of scallop myosin S1. Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11238-43. PMID:11016966 doi:10.1073/pnas.200376897

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dfk"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b7t|1b7t]], [[1dfl|1dfl]]</td></tr>
-<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=1dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dfk RCSB], [http://www.ebi.ac.uk/pdbsum/1dfk PDBsum]</span></td></tr>
+<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=1dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfk OCA], [http://pdbe.org/1dfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dfk RCSB], [http://www.ebi.ac.uk/pdbsum/1dfk PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYS_AEQIR MYS_AEQIR]] 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_AEQIR MLE_AEQIR]] 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_AEQIR MLR_AEQIR]] 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/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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1dfk" style="background-color:#fffaf0;"></div>
 ==See Also==

1dfk

From Proteopedia

Revision as of 04:13, 11 September 2015

NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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