Helppolainen Satu H, Määttä Juha A E, Halling Katrin K, Slotte J Peter, Hytönen Vesa P, Jänis Janne, Vainiotalo Pirjo, Kulomaa Markku S, Nordlund Henri R
Institute of Medical Technology, Biokatu 6, FI-33014 University of Tampere and Tampere University Hospital, Finland.
Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):1002-10. doi: 10.1016/j.bbapap.2008.04.010. Epub 2008 Apr 30.
A gene encoding an avidin-like protein was discovered in the genome of B. japonicum. The gene was cloned to an expression vector and a protein, named bradavidin II, was produced in E. coli. Bradavidin II has an identity of 20-30% and a similarity of 30-40% with previously discovered bradavidin and other avidin-like proteins. It has biochemical characteristics close to those of avidin and streptavidin and binds biotin tightly. In contrast to other tetrameric avidin-like proteins studied to date, bradavidin II has no tryptophan analogous to the W110 in avidin (W120 in streptavidin), thought to be one of the most essential residues for tight biotin-binding. Homology modeling suggests that a proline residue may function analogously to tryptophan in this particular position. Structural elements of bradavidin II such as an interface residue pattern or biotin contact residues could be used as such or transferred to engineered avidin forms to improve or create new tools for biotechnological applications.
在日本根瘤菌的基因组中发现了一个编码抗生物素蛋白样蛋白的基因。该基因被克隆到一个表达载体中，并在大肠杆菌中产生了一种名为布拉抗生物素蛋白II的蛋白质。布拉抗生物素蛋白II与先前发现的布拉抗生物素蛋白及其他抗生物素蛋白样蛋白的一致性为20%-30%，相似性为30%-40%。它具有与抗生物素蛋白和链霉抗生物素蛋白相近的生化特性，能紧密结合生物素。与迄今为止研究的其他四聚体抗生物素蛋白样蛋白不同，布拉抗生物素蛋白II没有类似于抗生物素蛋白中W110（链霉抗生物素蛋白中的W120）的色氨酸，而W110被认为是紧密结合生物素的最关键残基之一。同源建模表明，在这个特定位置脯氨酸残基可能发挥与色氨酸类似的功能。布拉抗生物素蛋白II的结构元件，如界面残基模式或生物素接触残基，可直接使用或转移到工程化抗生物素蛋白形式中，以改进或创造用于生物技术应用的新工具。
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