Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.

ABSTRACT: Site-directed spin labeling (SDSL) was used to examine and compare transmembrane signaling events in the bacterial outer-membrane transport proteins BtuB, FecA, and FhuA. These proteins extract energy for transport by coupling to the transperiplasmic protein TonB, an interaction that is thought to be mediated by the Ton box, a highly conserved energy-coupling motif in these transporters. In the ferric citrate transporter, FecA, SDSL indicates that the Ton box undergoes a substrate-induced disorder transition similar to that seen for BtuB, the vitamin B(12) transporter. This conformational change produces an aqueous exposed, highly disordered protein fragment, which likely regulates transporter-TonB interactions. However, in the ferrichrome transporter, FhuA, SDSL does not reveal a substrat

SUBMITTER: Kim M 

PROVIDER: S-EPMC1924579 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature