Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade

Abstract The thioredoxin (Trx)-coupled arsenate reductase (ArsC) is a family of enzymes that catalyzes the reduction of arsenate to arsenite in the arsenic detoxification pathway. The catalytic cycle involves a series of relayed intramolecular and intermolecular thiol-disulfide exchange reactions. S...

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Autores principales:	Wenbo Zhang, Xiaogang Niu, Jienv Ding, Yunfei Hu, Changwen Jin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Thiol-disulfide Exchange Reactions Chemical Exchange Saturation Transfer (CEST) Arscia CEST Experiments CEST Data Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f107f36c806848fe9ba43bb176dbaf44
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spelling	oai:doaj.org-article:f107f36c806848fe9ba43bb176dbaf442021-12-02T15:08:53ZIntra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade10.1038/s41598-018-33766-42045-2322https://doaj.org/article/f107f36c806848fe9ba43bb176dbaf442018-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-33766-4https://doaj.org/toc/2045-2322Abstract The thioredoxin (Trx)-coupled arsenate reductase (ArsC) is a family of enzymes that catalyzes the reduction of arsenate to arsenite in the arsenic detoxification pathway. The catalytic cycle involves a series of relayed intramolecular and intermolecular thiol-disulfide exchange reactions. Structures at different reaction stages have been determined, suggesting significant conformational fluctuations along the reaction pathway. Herein, we use two state-of-the-art NMR methods, the chemical exchange saturation transfer (CEST) and the CPMG-based relaxation dispersion (CPMG RD) experiments, to probe the conformational dynamics of B. subtilis ArsC in all reaction stages, namely the enzymatic active reduced state, the intra-molecular C10–C82 disulfide-bonded intermediate state, the inactive oxidized state, and the inter-molecular disulfide-bonded protein complex with Trx. Our results reveal highly rugged energy landscapes in the active reduced state, and suggest global collective motions in both the C10–C82 disulfide-bonded intermediate and the mixed-disulfide Trx-ArsC complex.Wenbo ZhangXiaogang NiuJienv DingYunfei HuChangwen JinNature PortfolioarticleThiol-disulfide Exchange ReactionsChemical Exchange Saturation Transfer (CEST)ArsciaCEST ExperimentsCEST DataMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Thiol-disulfide Exchange Reactions Chemical Exchange Saturation Transfer (CEST) Arscia CEST Experiments CEST Data Medicine R Science Q
spellingShingle	Thiol-disulfide Exchange Reactions Chemical Exchange Saturation Transfer (CEST) Arscia CEST Experiments CEST Data Medicine R Science Q Wenbo Zhang Xiaogang Niu Jienv Ding Yunfei Hu Changwen Jin Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
description	Abstract The thioredoxin (Trx)-coupled arsenate reductase (ArsC) is a family of enzymes that catalyzes the reduction of arsenate to arsenite in the arsenic detoxification pathway. The catalytic cycle involves a series of relayed intramolecular and intermolecular thiol-disulfide exchange reactions. Structures at different reaction stages have been determined, suggesting significant conformational fluctuations along the reaction pathway. Herein, we use two state-of-the-art NMR methods, the chemical exchange saturation transfer (CEST) and the CPMG-based relaxation dispersion (CPMG RD) experiments, to probe the conformational dynamics of B. subtilis ArsC in all reaction stages, namely the enzymatic active reduced state, the intra-molecular C10–C82 disulfide-bonded intermediate state, the inactive oxidized state, and the inter-molecular disulfide-bonded protein complex with Trx. Our results reveal highly rugged energy landscapes in the active reduced state, and suggest global collective motions in both the C10–C82 disulfide-bonded intermediate and the mixed-disulfide Trx-ArsC complex.
format	article
author	Wenbo Zhang Xiaogang Niu Jienv Ding Yunfei Hu Changwen Jin
author_facet	Wenbo Zhang Xiaogang Niu Jienv Ding Yunfei Hu Changwen Jin
author_sort	Wenbo Zhang
title	Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
title_short	Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
title_full	Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
title_fullStr	Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
title_full_unstemmed	Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
title_sort	intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/f107f36c806848fe9ba43bb176dbaf44
work_keys_str_mv	AT wenbozhang intraandinterproteincouplingsofbackbonemotionsunderlieproteinthioldisulfideexchangecascade AT xiaogangniu intraandinterproteincouplingsofbackbonemotionsunderlieproteinthioldisulfideexchangecascade AT jienvding intraandinterproteincouplingsofbackbonemotionsunderlieproteinthioldisulfideexchangecascade AT yunfeihu intraandinterproteincouplingsofbackbonemotionsunderlieproteinthioldisulfideexchangecascade AT changwenjin intraandinterproteincouplingsofbackbonemotionsunderlieproteinthioldisulfideexchangecascade
_version_	1718388036023091200

Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade

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