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Structural and functional studies of NirC from Salmonella typhimurium

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Rycovska-Blume,  Adriana
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Rycovska-Blume, A., Lü, W., Andrade, S., Fendler, K., & Einsle, O. (2015). Structural and functional studies of NirC from Salmonella typhimurium. In A. K. Shukla (Ed.), Methods in Enzymology (pp. 475-497). Amsterdam: Elsevier Inc.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-40FA-F
Abstract
NirC is a pentameric transport system for monovalent anions that is expressed in the context of assimilatory nitrite reductase NirBD in a wide variety of enterobacterial species. A NirC pentamer contains individual pores in each protomer that mediate the passage of at least the nitrite (NO2−) and nitrate (NO3−) anions. As a member of the formate/nitrite transporter family of membrane transport proteins, NirC shares a range of structural and functional features with the formate channel FocA and the hydrosulfide channel AsrD (HSC). NirC from the enteropathogen Salmonella typhimurium has been studied by X-ray crystallography, proton uptake assays, and different electrophysiological techniques, and the picture that has emerged shows a fast and versatile transport system for nitrite that doubles as a defense system during the enteric life of the bacterium. Structural and functional assays are described, which shed light on the transport mechanism of this important molecular machine