Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 477, Issue 1, Pages 20-26Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.06.014
Keywords
Redox switch; NMR; SAXS; Random coil; Secondary structure predictions; Disulfide bond
Categories
Funding
- French National Research Agency [ANR-13-BSV5-0013, ANR-08-JCJC-0036]
- joint fellowship CNRS-Region PACA
- TGIR-RMN-THC Fr3050 CNRS
- CNRS
- Aix-Marseille University
- A*Midex project [ANR-11-IDEX-0001-02]
- French National Research Agency (Signaux-BioNRJ) [ANR-15-CE05-0021-03]
- CNRS PEPS (Exo-Mod, DEBAT)
- Agence Nationale de la Recherche (ANR) [ANR-08-JCJC-0036, ANR-13-BSV5-0013] Funding Source: Agence Nationale de la Recherche (ANR)
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The redox switch protein CP12 is a key player of the regulation of the Benson-Calvin cycle. Its oxidation state is controlled by the formation/dissociation of two intramolecular disulphide bridges during the day/night cycle. CP12 was known to be globally intrinsically disordered on a large scale in its reduced state, while being partly ordered in the oxidised state. By combining Nuclear Magnetic Resonance and Small Angle X-ray Scattering experiments, we showed that, contrary to secondary structure or disorder predictions, reduced CP12 is fully disordered, with no transient or local residual structure likely to be precursor of the structures identified in the oxidised active state and/or in the bound state with GAPDH or PRK. These results highlight the diversity of the mechanisms of regulation of conditionally disordered redox switches, and question the stability of oxidised CP12 scaffold. (C) 2016 Elsevier Inc. All rights reserved.
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