Jensen Jaime L, Wu Qiong, Colbert Christopher L
Department of Chemistry and Biochemistry, North Dakota State University, Fargo, ND, 58102, USA.
Department of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN, 37240, USA.
Biomol NMR Assign. 2018 Apr;12(1):91-94. doi: 10.1007/s12104-017-9785-0. Epub 2017 Oct 25.
Outer membrane TonB-dependent transducers (TBDTs) actively transport ferric siderophore complexes from the extracellular environment into Gram-negative bacteria. They also participate in a cell-surface signaling regulatory pathway that results in upregulation of the transducer itself, in response to iron-deplete conditions. The TBDT PupB transports ferric pseudobactin, and signals through its N-terminal signaling domain (NTSD), while the TBDT homolog PupA is signaling-inactive. Here, we report the NMR chemical shift assignments of the PupB-NTSD. This information will provide the basis for structural characterization of the PupB-NTSD to further explore its signaling properties.
外膜中依赖TonB的转运蛋白（TBDTs）可将细胞外环境中的铁载体复合物主动转运到革兰氏阴性菌中。它们还参与一种细胞表面信号调节途径，在铁缺乏条件下，该途径会导致转运蛋白自身上调。TBDT PupB转运铁假菌素，并通过其N端信号结构域（NTSD）进行信号传导，而TBDT同源物PupA则无信号传导活性。在此，我们报告了PupB-NTSD的核磁共振化学位移归属。这些信息将为PupB-NTSD的结构表征提供基础，以进一步探索其信号传导特性。
