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首页> 外文期刊>Journal of synchrotron radiation >Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease
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Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease

机译：热稳定的膜结合型胃抑素特异性蛋白酶的结构和生化分析

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摘要

Membrane-bound proteases are involved in various regulatory functions. The N-terminal region of PH1510p (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p. In a form of human hemolytic anemia known as hereditary stomatocytosis, the stomatin protein is deficient in the erythrocyte membrane due to mis-trafficking. In order to understand the catalytic mechanism of 1510-N in more detail, here the structural and biochemical analysis of 1510-N is reported. Two degraded products were produced via acyl-enzyme intermediates. 1510-N is a thermostable protease, and thus crystallization after heat treatment of the protease-peptide complex was attempted in order to understand the catalytic mechanism of 1510-N. The structure after heat treatment is almost identical to that with no heat treatment. According to the superposition between the structures with heat treatment and with no heat treatment, the N-terminal half of the peptide is superposed well, whereas the C-terminal half of the peptide is slightly deviated. The N-terminal half of the peptide binds to 1510-N more tightly than the C-terminal half of the peptide. The flexible L2 loops of 1510-N cover the peptide, and are involved in the protease activity.
机译：膜结合蛋白酶参与各种调节功能。来自嗜热古细菌毕赤酵母（Pyrococcus horikoshii）的PH1510p（1510-N）的N端区域是带有催化Ser-Lys dyad（Ser97和Lys138）的丝氨酸蛋白酶，并特异性裂解p-stomatin PH1511p的C端疏水区域。 。在人类溶血性贫血的一种形式（称为遗传性造血细胞增多症）中，由于走私现象，stomatin蛋白在红细胞膜中缺乏。为了更详细地了解1510-N的催化机理，这里报道1510-N的结构和生化分析。通过酰基酶中间体产生两种降解产物。 1510-N是热稳定的蛋白酶，因此尝试对蛋白酶-肽复合物进行热处理后结晶，以了解1510-N的催化机理。热处理后的结构几乎与没有热处理的结构相同。根据经过热处理和不进行热处理的结构之间的重叠，肽的N-末端一半很好地重叠，而肽的C-末端一半略有偏离。肽的N末端一半比肽的C末端一半更紧密地结合1510-N。 1510-N的柔性L2环覆盖了肽段，并参与了蛋白酶的活性。

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