Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II.

Advances in Biophysics Pub Date : 1998-01-01
N Sasaki, K Sutoh
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引用次数: 0

Abstract

Three loop structures called the P-loop, switch I loop and switch II loop of myosin are major components of its ATPase site, and share structural and functional homology with the loop structures in other ATPases and GTPases such as kinesin and G-protein. Using the alanine scanning mutagenesis, structure-function relationship of the switch I and switch II loops in Dictyostelium myosin II was examined. Based on crystal structures of Dictyostelium myosin motor domain, functions of each residue in those loops are discussed.

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盘状盘基钢菌肌球蛋白二磷酸腺苷酶位点结构突变分析。
肌球蛋白的三个环结构分别为p环、开关I环和开关II环,是其atp酶位点的主要组成部分,与其他atp酶和gtp酶(如激酶和g蛋白)的环结构具有结构和功能上的同源性。利用丙氨酸扫描诱变技术,研究了盘形骨菌myosin II的开关I和开关II环的结构-功能关系。根据盘基骨菌肌球蛋白运动结构域的晶体结构,讨论了这些环中每个残基的功能。
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Preface Illegitimate recombination mediated by double-strand break and end-joining in Escherichia coli. Genetic and physiological regulation of non-homologous end-joining in mammalian cells. The function of RecQ helicase gene family (especially BLM) in DNA recombination and joining. Nijmegen breakage syndrome and DNA double strand break repair by NBS1 complex.
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