分辨率为2.5埃的羧肽酶A的马铃薯抑制剂复合物结构。
Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution.
作者信息
Rees D C, Lipscomb W N
出版信息
Proc Natl Acad Sci U S A. 1980 Aug;77(8):4633-7. doi: 10.1073/pnas.77.8.4633.
Abstract
The structure of the complex between the proteolytic enzyme carboxypeptidase A (peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) and the 39-amino-acid carboxypeptidase A inhibitor from potatoes has been determined at 2.5-A resolution. A combination of multiple isomorphous replacement, molecular replacement, and noncrystallographic symmetry averaging techniques was used to solve the structure. The chain trace of the inhibitor and details of the binding interactions in the complex are described. A surprising aspect of the complex is that the carboxy-terminal peptide bond of the inhibitor has been hydrolyzed, and the carboxy-terminal glycine is trapped in the binding pocket of carboxypeptidase A. Consequently, the complex resembles a stage in the catalytic mechanism after hydrolysis of the peptide bond. The ring of tyrosine-248, which is known to undergo large conformational changes upon substrate binding, is in the "down" position and interacts with the inhibitor in the complex.
摘要
已在2.5埃分辨率下确定了蛋白水解酶羧肽酶A（肽基-L-氨基酸水解酶，EC 3.4.17.1）与来自马铃薯的39个氨基酸的羧肽酶A抑制剂之间复合物的结构。采用多同晶置换、分子置换和非晶体学对称性平均技术相结合的方法来解析该结构。描述了抑制剂的链迹以及复合物中结合相互作用的细节。该复合物一个令人惊讶的方面是抑制剂的羧基末端肽键已被水解，羧基末端甘氨酸被困在羧肽酶A的结合口袋中。因此，该复合物类似于肽键水解后催化机制中的一个阶段。已知在底物结合时会发生大的构象变化的酪氨酸-248环处于“向下”位置，并在复合物中与抑制剂相互作用。
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