The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium-Reference-Cited by-同舟云学术

The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium

Published:2015-12-04 Issue:11 Volume:1 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Volbeda Anne¹^ORCID,Darnault Claudine¹,Renoux Oriane¹,Nicolet Yvain¹,Fontecilla-Camps Juan C.¹

Affiliation:

1. Metalloproteins Unit, Institut de Biologie Structurale, CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs CS10090, 38044 Grenoble, France.

Abstract

The dimerization of the O 2 sensor FNR is regulated by extremely fine-tuned interactions.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference33 articles.

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2. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: Exploiting the metabolic spectrum by controlling alternative gene programs;Körner H.;FEMS Microbiol. Rev.,2003

3. DNA binding and dimerization of the Fe−S-containing FNR protein from Escherichia coli are regulated by oxygen;Lazazzera B. A.;J. Biol. Chem.,1996

4. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding;Khoroshilova N.;Proc. Natl. Acad. Sci. U.S.A.,1995

5. Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro;Green J.;Biochem. J.,1996

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