Title |
NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB
|
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Published in |
Biomolecular NMR Assignments, October 2017
|
DOI | 10.1007/s12104-017-9785-0 |
Pubmed ID | |
Authors |
Jaime L. Jensen, Qiong Wu, Christopher L. Colbert |
Abstract |
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. |
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