1scm

From Proteopedia

(Difference between revisions)

Revision as of 07:01, 8 March 2018

STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION

Structural highlights

1scm is a 3 chain structure with sequence from Argir. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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. [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

The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

Structure of the regulatory domain of scallop myosin at 2.8 A resolution.,Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Gyorgyi AG, Cohen C Nature. 1994 Mar 24;368(6469):306-12. PMID:8127365^[1]

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

References

↑ Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Gyorgyi AG, Cohen C. Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature. 1994 Mar 24;368(6469):306-12. PMID:8127365 doi:http://dx.doi.org/10.1038/368306a0

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/1scm"

Categories: Argir | Cohen, C | Xie, X | Calcium-binding protein

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION==
 <StructureSection load='1scm' size='340' side='right' caption='[[1scm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1scm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Argir Argir]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SCM FirstGlance]. <br>
 </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='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=1scm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scm OCA], [http://pdbe.org/1scm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1scm RCSB], [http://www.ebi.ac.uk/pdbsum/1scm 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=1scm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scm OCA], [http://pdbe.org/1scm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1scm RCSB], [http://www.ebi.ac.uk/pdbsum/1scm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1scm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1scm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1scm_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1scm

From Proteopedia

Revision as of 07:01, 8 March 2018

STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox