两个“不相关”的依赖ATP的酶家族在其辅因子结合位点周围具有广泛的结构相似性。
Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites.
作者信息
Denessiouk K A, Lehtonen J V, Korpela T, Johnson M S
机构信息
Department of Biochemistry, University of Turku, Finland.
出版信息
Protein Sci. 1998 May;7(5):1136-46. doi: 10.1002/pro.5560070507.
Abstract
Two proteins, D-alanine:D-alanine ligase and cAMP-dependent protein kinase, share a remarkable degree of structural convergence despite having different three-dimensional folds and different enzymatic functions. Here we report that as many as 103 residues from 10 segments form two identical super-secondary structures between which the cofactor ATP is bound. The cofactor, two bound metal cations, and several water molecules form a large network of electrostatic and hydrophobic interactions common to both enzymes, and these are mediated by the similar placement of equivalent amino acids within the common supersecondary structures.
摘要
两种蛋白质，D-丙氨酸：D-丙氨酸连接酶和环磷酸腺苷依赖性蛋白激酶，尽管具有不同的三维折叠和不同的酶功能，但在结构上有显著程度的趋同。我们在此报告，来自10个片段的多达103个残基形成了两个相同的超二级结构，辅因子ATP结合在这两个结构之间。辅因子、两个结合的金属阳离子和几个水分子形成了两种酶共有的一个由静电和疏水相互作用构成的大网络，这些相互作用是由共同超二级结构内等效氨基酸的相似排布介导的。
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