1H, 13C and 15N resonance assignments of human muscle acylphosphatase
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
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DOI：
10.1007/s12104-011-9318-1
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发表时间：
2012-04-01
影响因子：
0.9
通讯作者：
Dobson, Christopher M.
中科院分区：
文献类型：
--
作者：
Fusco, Giuliana;De Simone, Alfonso;Dobson, Christopher M.
人肌肉酰基磷酸酶（mAcP）是一种具有铁氧还蛋白样拓扑结构的酶，其主要作用是水解酰基磷酸的羧基-磷酸键。该蛋白已被广泛用作阐明蛋白质折叠和错误折叠的分子决定因素的模型系统。在这里，我们提出了完整的NMR分配的骨架和侧链共振的mAcP与磷酸盐络合，从而提供了一个重要的资源，为未来的溶液状态的NMR光谱研究的结构和动力学的蛋白质折叠和错误折叠的背景下，这种蛋白质。
Human muscle acylphosphatase (mAcP) is an enzyme with a ferrodoxin-like topology whose primary role is to hydrolyze the carboxyl-phosphate bonds of acylphosphates. The protein has been widely used as a model system for elucidating the molecular determinants of protein folding and misfolding. We present here the full NMR assignments of the backbone and side chains resonances of mAcP complexed with phosphate, thus providing an important resource for future solution-state NMR spectroscopic studies of the structure and dynamics of this protein in the contexts of protein folding and misfolding.