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1s5g

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Revision as of 07:16, 8 March 2018

Structure of Scallop myosin S1 reveals a novel nucleotide conformation

Structural highlights

1s5g 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:	1qvi, 1kk8, 1kk7
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

Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near-rigor state (lever arm =45 degrees to the helical actin axis) shows the diphosphate moiety positioned on the surface of the nucleotide-binding pocket, rather than deep within it as had been observed previously. This conformation strongly suggests a specific mode of entry and exit of the nucleotide from the nucleotide-binding pocket through the so-called "front door." In addition, using a variety of scallop structures, including a relatively high-resolution 2.75-A nucleotide-free near-rigor structure, we have identified a conserved complex salt bridge connecting the 50-kDa upper and N-terminal subdomains. This salt bridge is present only in crystal structures of muscle myosin isoforms that exhibit a strong reciprocal relationship (also known as coupling) between actin and nucleotide affinity.

Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding.,Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:15184651^[1]

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

References

↑ Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C. Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:15184651 doi:10.1073/pnas.0403002101

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/1s5g"

@@ Line 1: / Line 1: @@
 ==Structure of Scallop myosin S1 reveals a novel nucleotide conformation==
 <StructureSection load='1s5g' size='340' side='right' caption='[[1s5g]], [[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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qvi|1qvi]], [[1kk8|1kk8]], [[1kk7|1kk7]]</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=1s5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5g OCA], [http://pdbe.org/1s5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s5g RCSB], [http://www.ebi.ac.uk/pdbsum/1s5g 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=1s5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5g OCA], [http://pdbe.org/1s5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s5g RCSB], [http://www.ebi.ac.uk/pdbsum/1s5g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s5g 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/s5/1s5g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s5g_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1s5g

From Proteopedia

Revision as of 07:16, 8 March 2018

Structure of Scallop myosin S1 reveals a novel nucleotide conformation

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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