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TitleAtomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.
Journal, issue, pagesCell, Vol. 97, Issue 4, Page 459-470, Year 1999
Publish dateMay 14, 1999
AuthorsA Houdusse / V N Kalabokis / D Himmel / A G Szent-Györgyi / C Cohen /
PubMed AbstractThe crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin ...The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A 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.
External linksCell / PubMed:10338210
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-1b7t:
MYOSIN DIGESTED BY PAPAIN
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • argopecten irradians (bay scallop)
KeywordsMYOSIN / MYOSIN MOTOR

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