1sr6

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[[Image:1sr6.gif|left|200px]]<br /><applet load="1sr6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sr6.gif|left|200px]]
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caption="1sr6, resolution 2.75&Aring;" />
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'''Structure of nucleotide-free scallop myosin S1'''<br />
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{{Structure
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|PDB= 1sr6 |SIZE=350|CAPTION= <scene name='initialview01'>1sr6</scene>, resolution 2.75&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Structure of nucleotide-free scallop myosin S1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SR6 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 <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR6 OCA].
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1SR6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15184651 15184651]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15184651 15184651]
[[Category: Argopecten irradians]]
[[Category: Argopecten irradians]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: scallop myosin s1]]
[[Category: scallop myosin s1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:36 2008''

Revision as of 12:08, 20 March 2008


PDB ID 1sr6

Drag the structure with the mouse to rotate
, resolution 2.75Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Structure of nucleotide-free scallop myosin S1


Overview

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.

About this Structure

1SR6 is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.

Reference

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

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