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NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB.

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.

SUBMITTER: Jensen JL

PROVIDER: S-EPMC5871555 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB.

Jensen Jaime L JL Wu Qiong Q Colbert Christopher L CL

Biomolecular NMR assignments 20171025 1

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 t ...[more]

PMID: 29071576

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