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  Structural and functional studies of NirC from Salmonella typhimurium

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.

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 Creators:
Rycovska-Blume, Adriana1, Author           
Lü, Wei2, Author
Andrade, Susana3, Author
Fendler, Klaus1, Author           
Einsle, Oliver3, Author
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Institute for Biochemistry, Albert-Ludwigs-University Freiburg, Freiburg im Breisgau, Germany, ou_persistent22              
3BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Freiburg im Breisgau, Germany, ou_persistent22              

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Free keywords: Nitrite channel; Dequenching assay; Acridine orange; Solid-supported membrane; Planar lipid bilayer; Crystal structure; Transport mechanism
 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

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Language(s): eng - English
 Dates: 2015
 Publication Status: Issued
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/bs.mie.2014.12.034
 Degree: -

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Title: Methods in Enzymology
  Subtitle : Membrane Proteins—Production and Functional Characterization
Source Genre: Series
 Creator(s):
Shukla, Arun K., Editor
Affiliations:
-
Publ. Info: Amsterdam : Elsevier Inc.
Pages: - Volume / Issue: 556 Sequence Number: - Start / End Page: 475 - 497 Identifier: ISBN: 978-0-12-8015216