Structural mechanism of disulphide bond-mediated redox switches

Journal of Biochemistry
Seong Eon Ryu

Abstract

The oxidation of cysteine sulphydryl in proteins produces sulphenic acid that can form a reversible disulphide bond with another cysteine. The disulphide bond formation often triggers switches in protein structure and activity, especially when the distance between the two cysteine sulphur atoms is longer than the resulting disulphide bond distance. As an early example for the reversible disulphide bond-mediated functional switches, the reduced and oxidized forms of the bacterial transcription factor OxyR were characterized by X-ray crystallography. Recently, the Drosophila vision signalling protein, the association of inactivation-no-afterpotential D (INAD) was analysed by structural and functional methods. The two conserved cysteines of INAD were found to cycle between reduced and oxidized states during the light signal processing in Drosophila eyes, which was achieved by conformation dependent modulation of the disulphide bond redox potential. The production of the hypertension control peptide angiotensins was also shown to be controlled by the reversible disulphide bond in the precursor protein angiotensinogen. The crystal structure of the complex of angiotensiongen with its processing enzyme renin elucidated the role of the...Continue Reading

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Citations

Jan 23, 2014·Chemical Reviews·Miriam Góngora-BenítezFernando Albericio
Jun 11, 2014·Acta Crystallographica. Section D, Biological Crystallography·Penchit ChitnumsubUbolsree Leartsakulpanich
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Oct 9, 2013·Acta Crystallographica. Section D, Biological Crystallography·David V SvintradzeH Tonie Wright
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Jun 10, 2014·Chemistry, an Asian Journal·Lin WangLi-Jun Wan
Jun 19, 2013·Chemical Communications : Chem Comm·Mary S CollinsDarren W Johnson

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