Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
Biochem Biophys Res Commun. 2011 Jan 28;404(4):1055-9. doi: 10.1016/j.bbrc.2010.12.109. Epub 2010 Dec 25.
Rap1 (repressor-activator protein 1) from Saccharomyces cerevisiae, containing a BRCT domain at its N-terminus, is a multifunctional protein that controls telomere function, silencing, and the activation of glycolytic and ribosomal protein genes. In this work, we determined the solution structure of Rap1 BRCT domain, which contains three β-strands and three α-helices. Structural comparison indicated that Rap1 BRCT domain adopts a global fold similar to other BRCT domains, implying some common structural aspects of BRCT domain family. On the other hand, Rap1 BRCT domain displays structural characteristics significantly different from other BRCT domains in that Rap1 BRCT domain adopts a rather flexible conformation with less secondary structure elements, revealing a novel fold of the BRCT domain family.
酿酒酵母 Rap1（阻遏物激活蛋白 1），其 N 端含有一个 BRCT 结构域，是一种多功能蛋白，它控制端粒功能、沉默和糖酵解及核糖体蛋白基因的激活。在本工作中，我们确定了 Rap1 BRCT 结构域的溶液结构，它包含三个β-折叠和三个α-螺旋。结构比较表明 Rap1 BRCT 结构域采用了与其他 BRCT 结构域相似的整体折叠，暗示了 BRCT 结构域家族的一些共同结构方面。另一方面，Rap1 BRCT 结构域显示出与其他 BRCT 结构域明显不同的结构特征，因为 Rap1 BRCT 结构域采用了相当灵活的构象，具有较少的二级结构元件，揭示了 BRCT 结构域家族的一种新折叠。
