Duncan T M, Cross R L
Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse 13210.
J Bioenerg Biomembr. 1992 Oct;24(5):453-61. doi: 10.1007/BF00762362.
An updated topological model is constructed for the catalytic nucleotide-binding site of the F1-ATPase. The model is based on analogies to the known structures of the MgATP site on adenylate kinase and the guanine nucleotide sites on elongation factor Tu (Ef-Tu) and the ras p21 protein. Recent studies of these known nucleotide-binding domains have revealed several common functional features and similar alignment of nucleotide in their binding folds, and these are used as a framework for evaluating results of affinity labeling and mutagenesis studies of the beta subunit of F1. Several potentially important residues on beta are noted that have not yet been studied by mutagenesis or affinity labeling.
为F1 - ATP酶的催化核苷酸结合位点构建了一个更新的拓扑模型。该模型基于与腺苷酸激酶上MgATP位点、延伸因子Tu(Ef - Tu)和ras p21蛋白上鸟嘌呤核苷酸位点已知结构的类比。最近对这些已知核苷酸结合结构域的研究揭示了几个共同的功能特征以及它们结合折叠中核苷酸的相似排列,这些被用作评估F1β亚基亲和标记和诱变研究结果的框架。文中指出了β上几个潜在重要的残基,尚未通过诱变或亲和标记进行研究。