Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.

ABSTRACT: TonB-dependent transporters (TBDTs) mediate energized transport of essential nutrients into gram-negative bacteria. TBDTs are increasingly being exploited for the delivery of antibiotics to drug-resistant bacteria. While much is known about ground state complexes of TBDTs, few details have emerged about the transport process itself. In this study, we exploit bacteriocin parasitization of a TBDT to probe the mechanics of transport. Previous work has shown that the N-terminal domain of Pseudomonas aeruginosa-specific bacteriocin pyocin S2 (PyoS2_NTD) is imported through the pyoverdine receptor FpvAI. PyoS2_NTD transport follows the opening of a proton-motive force-dependent pore through FpvAI and the delivery of its own TonB box that engages TonB. We use molecular

SUBMITTER: Goult JD 

PROVIDER: S-EPMC10994204 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature