来自孤挺花的假定腺苷酸环化酶 HpAC1 的晶体结构和酶学特性研究揭示了其主要的三磷酸酶活性。
Crystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity.
机构信息
Department of Biochemistry, University of Bayreuth, Universitaetsstr. 30, 95447 Bayreuth, Germany; Faculty of Chemistry and Chemical Biology, TU Dortmund and Drug Discovery Hub Dortmund (DDHD), Zentrum für Wirkstoffforschung (ZIW), Otto-Hahn-Strasse 4a, 44227 Dortmund, Germany.
Department of Biochemistry, University of Bayreuth, Universitaetsstr. 30, 95447 Bayreuth, Germany; MRC Laboratory of Molecular Biology (LMB), Francis Crick Avenue, CB2 0QH Cambridge, UK.
出版信息
J Struct Biol. 2020 Dec 1;212(3):107649. doi: 10.1016/j.jsb.2020.107649. Epub 2020 Oct 16.
HpAC1, a protein from Hippeastrum hybrid cultivars, was previously suggested to be a plant adenylyl cyclase. We describe a structural and enzymatic characterization of HpAC1. A crystal structure of HpAC1 in complex with a non-hydrolyzable GTP analog confirms a generic CYTH architecture, comprising a β-barrel with an internal substrate site. The structure reveals significant active site differences to AC proteins with CYTH fold, however, and we find that HpAC1 lacks measurable AC activity. Instead, HpAC1 has substantial triphosphatase activity, indicating this protective activity or a related activity as the protein's physiological function.
HpAC1 是一种来自朱顶红杂交品种的蛋白质，先前被认为是一种植物腺苷酸环化酶。我们描述了 HpAC1 的结构和酶学特性。HpAC1 与非水解 GTP 类似物复合物的晶体结构证实了通用的 CYTH 结构，包括一个带有内部底物结合位点的 β-桶。然而，该结构显示出与具有 CYTH 折叠的 AC 蛋白显著不同的活性位点差异，我们发现 HpAC1 缺乏可测量的 AC 活性。相反，HpAC1 具有显著的三磷酸酶活性，表明这种保护活性或相关活性是该蛋白的生理功能。
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