Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue-Strasse 9, 60438 Frankfurt/Main, Germany.
Structure. 2011 Apr 13;19(4):577-87. doi: 10.1016/j.str.2011.01.012.
The Rcs-signaling system is one of the most remarkable phosphorelay pathways in Enterobacteriaceae, comprising several membrane-bound and soluble proteins. Within the complex phosphotransfer pathway, the histidine phosphotransferase (HPt) domain of the RcsD membrane-bound component serves as a crucial factor in modulating the phosphorylation state of the transcription factor RcsB. We have identified a new domain, RcsD-ABL, located N terminally to RcsD-HPt that interacts with RcsB as well. We have determined its structure, characterized its interaction interface with RcsB, and built a structural model of the complex of the RcsD-ABL domain with RcsB. Our results indicate that the effector domain of RcsB, which normally binds to DNA, is recognized by RcsD-ABL, whereas the HPt domain interacts with the phosphoreceiver domain of RcsB.
Rcs 信号系统是肠杆菌科中最显著的磷酸接力途径之一，包含几个膜结合和可溶性蛋白。在复杂的磷酸转移途径中，RcsD 膜结合成分的组氨酸磷酸转移酶（HPt）结构域是调节转录因子 RcsB 磷酸化状态的关键因素。我们已经鉴定出 RcsD-HPt N 端的一个新结构域 RcsD-ABL，它与 RcsB 相互作用。我们确定了它的结构，表征了它与 RcsB 的相互作用界面，并构建了 RcsD-ABL 结构域与 RcsB 复合物的结构模型。我们的结果表明，RcsB 的效应子结构域通常与 DNA 结合，被 RcsD-ABL 识别，而 HPt 结构域与 RcsB 的磷酸受体结构域相互作用。
