Brosey Chris A, Chagot Marie-Eve, Ehrhardt Mark, Pretto Dalyir I, Weiner Brian E, Chazin Walter J
Department of Biochemistry, and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, USA.
J Am Chem Soc. 2009 May 13;131(18):6346-7. doi: 10.1021/ja9013634.
Modular proteins with multiple domains tethered by flexible linkers have variable global architectures. Using the eukaryotic ssDNA binding protein, Replication Protein A (RPA), we demonstrate that NMR spectroscopy is a powerful tool to characterize the remodeling of architecture in different functional states. The first direct evidence is obtained for the remodeling of RPA upon binding ssDNA, including an alteration in the availability of the RPA32N domain that may help explain its damage-dependent phosphorylation.
由柔性接头连接的具有多个结构域的模块化蛋白质具有可变的整体结构。利用真核单链DNA结合蛋白复制蛋白A（RPA），我们证明核磁共振波谱是表征不同功能状态下结构重塑的有力工具。我们获得了RPA结合单链DNA时重塑的首个直接证据，包括RPA32N结构域可用性的改变，这可能有助于解释其损伤依赖性磷酸化。
