DMCA
Glycine 699 is Pivotal for the Motor Activity of Skeletal Muscle Myosin
| Citations: | 11 - 1 self |
BibTeX
@MISC{Kinose_glycine699,
author = {Fumi Kinose and Sharon X. Wang and Usha S. Kidambi and Carole L. Moncman and Donald A. Winkelmann},
title = {Glycine 699 is Pivotal for the Motor Activity of Skeletal Muscle Myosin},
year = {}
}
Share
 |
 |
 |
 |
||
OpenURL
Abstract
Abstract. Myosin couples ATP hydrolysis to the translocation of actin filaments to power many forms of cellular motility. A striking feature of the structure of the muscle myosin head domain is a 9-nm long "lever arm" that has been postulated to produce a 5-10-nm power stroke. This motion must be coupled to conformational changes around the actin and nucleotide binding sites. The linkage of these sites to the lever arm has been analyzed by site-directed mutagenesis of a conserved glycine residue (G699) found in a bend joining two helices containing the highly reactive and mobile cysteine residues, SH1 and SH2. Alanine mutagenesis of this glycine (G699A) dramatically alters the motor activity of skeletal muscle myosin, inhibiting the velocity of actin filament movement by>100-fold. Analysis of the defect
Keyphrases
motor activity skeletal muscle myosin power many form cellular motility actin filament 5-10-nm power stroke muscle myosin head domain lever arm alanine mutagenesis conformational change site-directed mutagenesis mobile cysteine residue atp hydrolysis conserved glycine residue nucleotide binding site 9-nm long lever arm striking feature actin filament movement
