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Structural and Functional Studies of NirC from Salmonella typhimurium.
- 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.)
- Subjects :
- Crystallography, X-Ray methods
Humans
Models, Molecular
Protein Conformation
Salmonella Infections microbiology
Salmonella typhimurium metabolism
Anion Transport Proteins chemistry
Anion Transport Proteins metabolism
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Salmonella typhimurium chemistry
Subjects
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