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3i5f

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Revision as of 09:41, 19 December 2018

Crystal structure of squid MG.ADP myosin S1

Structural highlights

3i5f is a 3 chain structure with sequence from Loligo pealei and Todarodes pacificus. This structure supersedes the now removed PDB entry 2oy6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2oy6, 3i5g, 3i5h, 3i5i
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MLE_TODPA] 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_TODPA] 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

Unlike processive cellular motors such as myosin V, whose structure has recently been determined in a "rigor-like" conformation, myosin II from contracting muscle filaments necessarily spends most of its time detached from actin. By using squid and sea scallop sources, however, we have now obtained similar rigor-like atomic structures for muscle myosin heads (S1). The significance of the hallmark closed actin-binding cleft in these crystal structures is supported here by actin/S1-binding studies. These structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of detailed differences in interdomain contacts. Moreover, the rigor-like position of switch II turns out to be unique for myosin V. The overall arrangements of subdomains in the motor are relatively conserved in each of the known contractile states, and we explore qualitatively the energetics of these states.

Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor.,Yang Y, Gourinath S, Kovacs M, Nyitray L, Reutzel R, Himmel DM, O'Neall-Hennessey E, Reshetnikova L, Szent-Gyorgyi AG, Brown JH, Cohen C Structure. 2007 May;15(5):553-64. PMID:17502101^[1]

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

References

↑ Yang Y, Gourinath S, Kovacs M, Nyitray L, Reutzel R, Himmel DM, O'Neall-Hennessey E, Reshetnikova L, Szent-Gyorgyi AG, Brown JH, Cohen C. Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor. Structure. 2007 May;15(5):553-64. PMID:17502101 doi:10.1016/j.str.2007.03.010

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/3i5f"

@@ Line 1: / Line 1: @@
 ==Crystal structure of squid MG.ADP myosin S1==
 <StructureSection load='3i5f' size='340' side='right' caption='[[3i5f]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oy6|2oy6]], [[3i5g|3i5g]], [[3i5h|3i5h]], [[3i5i|3i5i]]</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=3i5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5f OCA], [http://pdbe.org/3i5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i5f RCSB], [http://www.ebi.ac.uk/pdbsum/3i5f 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=3i5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5f OCA], [http://pdbe.org/3i5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i5f RCSB], [http://www.ebi.ac.uk/pdbsum/3i5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i5f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/3i5f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/3i5f_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 50: / Line 51: @@
 [[Category: Actin-binding]]
 [[Category: Atp-binding]]
+[[Category: Calcium]]
+[[Category: Coiled coil]]
 [[Category: Contractile protein]]
 [[Category: Mg adp]]

3i5f

From Proteopedia

Revision as of 09:41, 19 December 2018

Crystal structure of squid MG.ADP myosin S1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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