1s5g: Difference between revisions

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[[Image:1s5g.gif|left|200px]]
{{Seed}}
[[Image:1s5g.png|left|200px]]


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{{STRUCTURE_1s5g|  PDB=1s5g  |  SCENE=  }}  
{{STRUCTURE_1s5g|  PDB=1s5g  |  SCENE=  }}  


'''Structure of Scallop myosin S1 reveals a novel nucleotide conformation'''
===Structure of Scallop myosin S1 reveals a novel nucleotide conformation===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_15184651}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15184651}}


==About this Structure==
==About this Structure==
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[[Category: Novel conformation of nucleotide]]
[[Category: Novel conformation of nucleotide]]
[[Category: Scallop myosin s1]]
[[Category: Scallop myosin s1]]
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