Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscle.

ABSTRACT: The orientation of the ELC region of myosin in skeletal muscle was determined by polarized fluorescence from ELC mutants in which pairs of introduced cysteines were cross-linked by BSR. The purified ELC-BSRs were exchanged for native ELC in demembranated fibers from rabbit psoas muscle using a trifluoperazine-based protocol that preserved fiber function. In the absence of MgATP (in rigor) the ELC orientation distribution was narrow; in terms of crystallographic structures of the myosin head, the LCD long axis linking heavy-chain residues 707 and 843 makes an angle (beta) of 120-125 degrees with the filament axis. This is approximately 30 degrees larger than the broader distribution determined previously from RLC probes, suggesting that, relative to crystallographic structures, the LCD is b

SUBMITTER: Knowles AC 

PROVIDER: S-EPMC2553117 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature