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1sr6

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(New page: 200px<br /><applet load="1sr6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sr6, resolution 2.75&Aring;" /> '''Structure of nucleot...)
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[[Image:1sr6.gif|left|200px]]<br /><applet load="1sr6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sr6.gif|left|200px]]<br /><applet load="1sr6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sr6, resolution 2.75&Aring;" />
caption="1sr6, resolution 2.75&Aring;" />
'''Structure of nucleotide-free scallop myosin S1'''<br />
'''Structure of nucleotide-free scallop myosin S1'''<br />
==Overview==
==Overview==
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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.
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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==
==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 SO4, MG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SR6 OCA].
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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].
==Reference==
==Reference==
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[[Category: Cohen, C.]]
[[Category: Cohen, C.]]
[[Category: Gourinath, S.]]
[[Category: Gourinath, S.]]
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[[Category: Himmel, D.M.]]
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[[Category: Himmel, D M.]]
[[Category: Risal, D.]]
[[Category: Risal, D.]]
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[[Category: Szent-Gyorgyi, A.G.]]
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[[Category: Szent-Gyorgyi, A G.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MG]]
[[Category: MG]]
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[[Category: scallop myosin s1]]
[[Category: scallop myosin s1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:35:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:21 2008''

Revision as of 13:04, 21 February 2008


1sr6, resolution 2.75Å

Drag the structure with the mouse to rotate

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 with , and as ligands. 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

Page seeded by OCA on Thu Feb 21 15:04:21 2008

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