枯草杆菌蛋白酶样蛋白的结构催化核心及其与胰蛋白酶样丝氨酸蛋白酶和 α/β-水解酶的比较。

Structural Bioinformatics Laboratory, Biochemistry, InFLAMES Research Flagship Center, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.

Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.

Int J Mol Sci. 2024 Nov 5;25(22):11858. doi: 10.3390/ijms252211858.

Subtilisin-like proteins are serine proteases that use two types of catalytic triads: Ser-His-Asp and Ser-Glu-Asp. Here, we investigate the two known families of subtilisin-like proteins, the subtilases (Ser-His-Asp triad) and the serine-carboxyl proteinases (Ser-Glu-Asp triad), and describe the local structural arrangements (cores) that govern the catalytic residues in these proteins. We show the separation of the cores into conserved structural zones, which can be repeatedly found in different structures, and compare the structural cores in subtilisin-like proteins with those in trypsin-like serine proteases and alpha/beta-hydrolases.

类枯草杆菌蛋白酶是丝氨酸蛋白酶，使用两种类型的催化三联体：Ser-His-Asp 和 Ser-Glu-Asp。在这里，我们研究了两种已知的类枯草杆菌蛋白酶家族，即枯草杆菌蛋白酶（Ser-His-Asp 三联体）和丝氨酸羧基蛋白酶（Ser-Glu-Asp 三联体），并描述了控制这些蛋白质中催化残基的局部结构排列（核心）。我们将核心分为保守的结构区域，这些区域可以在不同的结构中反复找到，并将类枯草杆菌蛋白酶中的结构核心与胰蛋白酶样丝氨酸蛋白酶和 α/β-水解酶中的结构核心进行比较。