Nucleotide-induced movements in the myosin head near the converter region.
B Pliszka, E Karczewska, B Wawro
Index: Biochim. Biophys. Acta 1481(1) , 55-62, (2000)
Full Text: HTML
Abstract
Structural changes in subfragment 1 of skeletal muscle myosin were investigated by cross-linking trypsin-cleaved S1 with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. In the absence of nucleotide the alkali light chains are cross-linked to the 27 kDa heavy chain fragment; the presence of MgATP reduces the efficiency of this reaction. On the other hand, MgATP promotes the cross-link formation between the N-terminal 27 kDa and C-terminal 20 kDa fragments of the heavy chain. The chemical cleavage of the cross-linked heavy chains fragments with N-chlorosuccinimide and hydroxylamine indicates that the cross-links are formed between the regions spanning residues 131-204 and 699-809. These results indicate that the two regions of the heavy chain that are relatively distant in nucleotide-free skeletal S1 [Rayment et al. (1993) Science 261, 50-58] can potentially interact upon addition of nucleotide.
Related Compounds
Related Articles:
2004-11-15
[J. Chem. Phys. 121(19) , 9489-97, (2004)]
2010-09-01
[J. Fluoresc. 20(5) , 1061-8, (2010)]
1998-03-20
[J. Chromatogr. B. Biomed. Sci. Appl. 706(2) , 191-9, (1998)]
1990-11-05
[J. Biol. Chem. 265(31) , 18786-90, (1990)]
1996-08-01
[J. Pharm. Biomed. Anal. 14(11) , 1579-84, (1996)]