Crystal structures of the photosystem II D1 C-terminal processing protease
Crystal structures of the photosystem II D1 C-terminal processing protease
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DOI：
10.1038/78973
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发表时间：
2000-09-01
期刊：
影响因子：
--
通讯作者：
Diner, BA
中科院分区：
文献类型：
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作者：
Liao, DI;Qian, J;Diner, BA
我们在这里报告的第一个三维结构的D1 C-末端加工蛋白酶（DIP），这是由ctpA基因编码。这种酶去除了产氧光合作用的光系统II的D1多肽的C-末端延伸。蛋白水解加工是允许四核锰簇的光驱动组装所必需的，所述四核锰簇负责光合水氧化。用多波长反常色散法测定了栅藻酶的X射线结构，分辨率为1.8埃。该酶是单体的，由三个折叠结构域组成。中间结构域与已知的PDZ基序拓扑同源，并被认为是底物C-末端结合的位点。底物的其余部分可能延伸穿过酶的表面，在其易断裂的键处与酶活性位点Ser 372/Lys 397催化染色相互作用，该酶活性位点位于三个结构域界面处的蛋白质中心。
We report here the first three-dimensional structure of the D1 C-terminal processing protease (DIP), which is encoded by the ctpA gene. This enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II of oxygenic photosynthesis, Proteolytic processing is necessary to allow the light driven assembly of the tetranuclear manganese duster, which is responsible for photosynthetic water oxidation. The X-ray structure of the Scenedesmus obliquus enzyme has been determined at 1.8 Angstrom resolution using the multiwavelength anomalous dispersion method. The enzyme is monomeric and is composed of three folding domains. The middle domain is topologically homologous to known PDZ motifs and is proposed to be the site at which the substrate C-terminus binds. The remainder of the substrate likely extends across the face of the enzyme, interacting at its scissile bond with the enzyme active site Ser 372/Lys 397 catalytic dyed, which lies at the center of the protein at the interface of the three domains.