Alternative Model for RND-Type Efflux Pump
AUTOR(ES)
Torres, Pedro Henrique Monteiro, Pascutti, Pedro Geraldo, Bisch, Paulo Mascarello, Silva, Manuela Leal da
FONTE
J. Braz. Chem. Soc.
DATA DE PUBLICAÇÃO
2016-12
RESUMO
RND (resistance-nodulation-division) transporters are found in several Gram-negative bacteria species. These proteins form a complex along with membrane fusion proteins and outer membrane factors. This complex acts as an efflux pump, transporting several different molecules directly from the cytoplasm to the extracellular medium. Although the crystallographic structure of each protein of the complex is known, the complete complex assembly is not yet fully characterized. In 2014, a model for the complete system, based upon a cryoelectron-microscopy map, was proposed. In the present work, we propose an alternative model that also satisfies the volume obtained from the cryoelectron-microscopy assay. In this model, the AcrA helical domains are interleaved to the helical domains of the TolC protein, increasing the diameter of the formed pore. We believe that this model represents a better model for RND-type efflux pump and might contribute to the characterization of this system.
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