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| {{STRUCTURE_1s5g| PDB=1s5g | SCENE= }} | | {{STRUCTURE_1s5g| PDB=1s5g | SCENE= }} |
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| '''Structure of Scallop myosin S1 reveals a novel nucleotide conformation'''
| | ===Structure of Scallop myosin S1 reveals a novel nucleotide conformation=== |
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| ==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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15184651 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15184651}} |
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| ==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]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:19:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:46:39 2008'' |