Smooth Muscle Myosin
作者： Hirofumi Onishi , Manuel F. Morales , Shin-ichiro Kojima , Kazuo Katoh , Keigi Fujiwara
DOI: 10.1007/978-1-4684-6039-1_12
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摘要: From their crystallographic comparisons, Fisher et al. (Biochemistry 34, 8960-8972, 1995) have proposed that in an important transition of myosin heads (M), MATP → M ADP Pi, interdomain rotation occurs Gly468 (of chicken smooth muscle myosin) and the rotated state is stabilized by newly-formed contacts including salt link between Glu470 Arg247 myosin). Here, we studied effects Gly468, Glu470, mutations on hydrolysis ATP. The G468A HMM did not show a significant ATPase activity, stoichiometric initial phosphate burst, tryptophan fluorescence enhancement attributed to bound Pi. E470A also activity but mutant gave response E470R/R247E exhibited burst which were comparable those wild-type HMM, whereas neither E470R nor R247E showed such burst. We thus propose both unhindered stabilizes are necessary for ATP hydrolysis.
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