Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state

Hélène Launay; Patrick Barré; Carine Puppo; Stéphanie Manneville; Brigitte Gontero; Véronique Receveur-Bréchot

doi:10.1016/j.bbrc.2016.06.014

Journal articles

Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state

Hélène Launay ^{1, 2} Patrick Barré ³ Carine Puppo ⁴ Stéphanie Manneville ⁵ Brigitte Gontero ⁴ Véronique Receveur-Bréchot ^{6, 7}

1 UGSF - Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576

2 Université de Lille

3 LGE - Laboratoire de géologie de l'ENS

4 BIP - Bioénergétique et Ingénierie des Protéines

5 Phys-ENS - Laboratoire de Physique de l'ENS Lyon

6 Institut Paoli-Calmettes

7 AMU - Aix Marseille Université

Abstract : 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.

Keywords : Redox switch NMR SAXS Random coil Secondary structure predictions Disulfide bond

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Journal articles

Domain :

Life Sciences [q-bio]

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Submitted on : Tuesday, January 10, 2017 - 1:51:46 PM
Last modification on : Wednesday, October 14, 2020 - 3:47:33 AM

Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state

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Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state

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