Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head
The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 Å resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre–power...
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| Veröffentlicht in: | Cell 1999-05, Vol.97 (4), p.459-470 |
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| creator | Houdusse, Anne Kalabokis, Vassilios N. Himmel, Daniel Szent-Györgyi, Andrew G. Cohen, Carolyn |
| description | The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 Å resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre–power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible “joints” produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis (“ATP”) states of the contractile cycle in which the myosin heads stay detached from actin. |
| doi_str_mv | 10.1016/S0092-8674(00)80756-4 |
| format | Article |
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The converter and the lever arm are in very different positions from those in either the pre–power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible “joints” produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. 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The converter and the lever arm are in very different positions from those in either the pre–power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible “joints” produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis (“ATP”) states of the contractile cycle in which the myosin heads stay detached from actin.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10338210</pmid><doi>10.1016/S0092-8674(00)80756-4</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals |
| subjects | Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Amino Acid Sequence Animals Binding Sites Bivalvia Crystallography, X-Ray Marine Models, Molecular Molecular Sequence Data Mollusca - chemistry Myosins - chemistry Myosins - metabolism Phosphates Protein Conformation |
| title | Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head |
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