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Structural and Functional Studies of NirC from Salmonella typhimurium.

Authors :
Rycovska-Blume A
Lü W
Andrade S
Fendler K
Einsle O
Source :
Methods in enzymology [Methods Enzymol] 2015; Vol. 556, pp. 475-97. Date of Electronic Publication: 2015 Mar 20.
Publication Year :
2015

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 [Formula: see text] and nitrate [Formula: see text] 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.<br /> (© 2015 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1557-7988
Volume :
556
Database :
MEDLINE
Journal :
Methods in enzymology
Publication Type :
Academic Journal
Accession number :
25857796
Full Text :
https://doi.org/10.1016/bs.mie.2014.12.034