Glycine 699 is Pivotal for the Motor Activity of Skeletal Muscle Myosin

Content Provider	CiteSeerX
Author	Wang, Sharon X. Moncman, Carole L. Kidambi, Usha S. Winkelmann, Donald A. Kinose, Fumi
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
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Subject Keyword	Site-directed Mutagenesis Mobile Cysteine Residue Conserved Glycine Residue Actin Filament Muscle Myosin Head Domain Actin Filament Movement Alanine Mutagenesis Skeletal Muscle Myosin Motor Activity Atp Hydrolysis Nucleotide Binding Site 5-10-nm Power Stroke Lever Arm 9-nm Long Lever Arm Cellular Motility Conformational Change Striking Feature Power Many Form
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