Dodecin sequesters FAD in closed conformation from the aqueous solution
Dodecin sequesters FAD in closed conformation from the aqueous solution
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DOI：
10.1016/j.jmb.2006.08.083
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发表时间：
2006-12-08
影响因子：
5.6
通讯作者：
Oesterhelt, Dieter
中科院分区：
文献类型：
--
作者：
Grininger, Martin;Seiler, Florian;Oesterhelt, Dieter
无论是广泛的理论计算和几十年来获得的实验数据留下的黄素腺嘌呤二核苷酸（FAD）在水溶液中存在的开放以及在一个封闭的构象毫无疑问。然而，关于FAD的分子内堆积复合物的知识是建立在间接的方法上，而缺乏直接的结构证据。最近，十二碳苷被报道为非特异性黄素结合蛋白，其表现出将黄素的堆叠二聚体并入单个结合口袋的独特结合模式。在这里，我们表明，FAD是不是以这种方式结合，但在单体的分子内堆叠构象。由于十二碳配体结合特性，这种FAD堆叠构象表明直接从水溶液中分离，因此是FAD溶液堆叠形式的第一个X射线结构视图。此外，在非凡的FAD结合中，十二碳苷作为研究结合单体（FAD）与结合二聚体（例如核黄素）黄素性质的模型。(c)2006爱思唯尔有限公司版权所有。
Both extensive theoretical calculations and experimental data obtained during several decades leave little doubt that flavin adenine dinucleotide (FAD) exists in an open as well as in a closed conformation in aqueous solution. However, the knowledge about the intramolecularly stacked complex of FAD is constructed on indirect methods while direct structural evidence is lacking. Recently, dodecin was reported as an unspecific flavin binding protein which exhibits the unique binding mode of incorporating stacked dimers of flavins into a single binding pocket. Here, we show that FAD is not bound in this manner, but in monomers of intramolecularly stacked conformation. As resulting from the dodecin ligand binding characteristic, this FAD stacked conformation suggests to be directly sequestered from the aqueous solution and thus to be the first X-ray structural view on a FAD solution-stacked form. Moreover, in extraordinary FAD binding, dodecin serves as a model for studying bound monomeric (FAD) versus bound dimeric (e.g. riboflavin) flavin properties. (c) 2006 Elsevier Ltd. All rights reserved.