Structural and Metal Binding Characterization of the C-Terminal Metallochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34-Reference-Cited by-同舟云学术

Structural and Metal Binding Characterization of the C-Terminal Metallochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34

Published:2011-02-22 Issue:12 Volume:50 Page:2194-2204
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bersch Beate¹,Derfoufi Kheiro-Mouna²,De Angelis Fabien²,Auquier Vanessa²,Ngonlong Ekendé Elisabeth²,Mergeay Max³,Ruysschaert Jean-Marie²,Vandenbussche Guy²

Affiliation:

1. CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France, CEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France, and Université Grenoble 1, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France

2. Laboratory for the Structure and Function of Biological Membranes, Center for Structural Biology and Bioinformatics, Université Libre de Bruxelles, B-1050 Bruxelles, Belgium

3. Molecular and Cellular Biology, Belgian Center for Nuclear Energy, SCK·CEN, B-2400 Mol, Belgium

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200005k

Reference70 articles.

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3. Czc/Cnr efflux: a three-component chemiosmotlc antiport pathway with a 12-transmembrane-helix protein

4. Ion efflux systems involved in bacterial metal resistances

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