1s5g: Difference between revisions

Revision as of 15:58, 21 February 2008

Structure of Scallop myosin S1 reveals a novel nucleotide conformation

OverviewOverview

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 StructureAbout this Structure

1S5G is a Protein complex structure of sequences from Argopecten irradians with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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 14:58:09 2008

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OCA

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-[[Image:1s5g.gif|left|200px]]<br /><applet load="1s5g" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1s5g.gif|left|200px]]<br /><applet load="1s5g" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1s5g, resolution 3.1&Aring;" />
 '''Structure of Scallop myosin S1 reveals a novel nucleotide conformation'''<br />
 ==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.
+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==
-S5G 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, CA, MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S5G OCA].
+S5G 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=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5G OCA].
 ==Reference==
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 [[Category: Cohen, C.]]
 [[Category: Gourinath, S.]]
-[[Category: Himmel, D.M.]]
+[[Category: Himmel, D M.]]
 [[Category: Risal, D.]]
-[[Category: Szent-Gyorgyi, A.G.]]
+[[Category: Szent-Gyorgyi, A G.]]
 [[Category: ADP]]
 [[Category: CA]]
@@ Line 27: / Line 27: @@
 [[Category: scallop myosin s1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:07:27 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:09 2008''