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Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis

Nandita Bodra UGent, David Young, Leonardo Astolfi Rosado, Anna Pallo, Khadija Wahni, Frank De Proft, Jingjing Huang UGent, Frank Van Breusegem UGent and Joris Messens (2017) SCIENTIFIC REPORTS. 7.
abstract
Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress. DHAR enzymes bear close structural homology to the glutathione transferase (GST) superfamily of enzymes and contain the same active site motif, but most GSTs do not exhibit DHAR activity. The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Here we present the crystal structure of DHAR2 from Arabidopsis thaliana with GSH bound to the catalytic cysteine. This structure reveals localized conformational differences around the active site which distinguishes the GSH-bound DHAR2 structure from that of DHAR1. We also unraveled the enzymatic step in which DHAR releases oxidized glutathione (GSSG). To consolidate our structural and kinetic findings, we investigated potential conformational flexibility in DHAR2 by normal mode analysis and found that subdomain mobility could be linked to GSH binding or GSSG release.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
GLUTATHIONE TRANSFERASE P1-1, PERFORMANCE LIQUID-CHROMATOGRAPHY, MOLECULAR-DYNAMICS SIMULATIONS, INDUCED-FIT MECHANISM, NORMAL-MODE, ANALYSIS, SULFENIC ACID, WEB SERVER, POPULUS-TRICHOCARPA, ASCORBIC-ACID, NETWORK MODEL
journal title
SCIENTIFIC REPORTS
Sci. Rep.
volume
7
article number
42494
pages
10 pages
Web of Science type
Article
Web of Science id
000393942700002
ISSN
2045-2322
DOI
10.1038/srep42494
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
id
8516847
handle
http://hdl.handle.net/1854/LU-8516847
date created
2017-04-04 10:05:17
date last changed
2017-05-16 11:32:17
@article{8516847,
  abstract     = {Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress. DHAR enzymes bear close structural homology to the glutathione transferase (GST) superfamily of enzymes and contain the same active site motif, but most GSTs do not exhibit DHAR activity. The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Here we present the crystal structure of DHAR2 from Arabidopsis thaliana with GSH bound to the catalytic cysteine. This structure reveals localized conformational differences around the active site which distinguishes the GSH-bound DHAR2 structure from that of DHAR1. We also unraveled the enzymatic step in which DHAR releases oxidized glutathione (GSSG). To consolidate our structural and kinetic findings, we investigated potential conformational flexibility in DHAR2 by normal mode analysis and found that subdomain mobility could be linked to GSH binding or GSSG release.},
  articleno    = {42494},
  author       = {Bodra, Nandita and Young, David and Rosado, Leonardo Astolfi and Pallo, Anna and Wahni, Khadija and De Proft, Frank and Huang, Jingjing and Van Breusegem, Frank and Messens, Joris},
  issn         = {2045-2322},
  journal      = {SCIENTIFIC REPORTS},
  keyword      = {GLUTATHIONE TRANSFERASE P1-1,PERFORMANCE LIQUID-CHROMATOGRAPHY,MOLECULAR-DYNAMICS SIMULATIONS,INDUCED-FIT MECHANISM,NORMAL-MODE,ANALYSIS,SULFENIC ACID,WEB SERVER,POPULUS-TRICHOCARPA,ASCORBIC-ACID,NETWORK MODEL},
  language     = {eng},
  pages        = {10},
  title        = {Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis},
  url          = {http://dx.doi.org/10.1038/srep42494},
  volume       = {7},
  year         = {2017},
}

Chicago
Bodra, Nandita, David Young, Leonardo Astolfi Rosado, Anna Pallo, Khadija Wahni, Frank De Proft, Jingjing Huang, Frank Van Breusegem, and Joris Messens. 2017. “Arabidopsis Thaliana Dehydroascorbate Reductase 2 : Conformational Flexibility During Catalysis.” Scientific Reports 7.
APA
Bodra, N., Young, D., Rosado, L. A., Pallo, A., Wahni, K., De Proft, F., Huang, J., et al. (2017). Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis. SCIENTIFIC REPORTS, 7.
Vancouver
1.
Bodra N, Young D, Rosado LA, Pallo A, Wahni K, De Proft F, et al. Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis. SCIENTIFIC REPORTS. 2017;7.
MLA
Bodra, Nandita, David Young, Leonardo Astolfi Rosado, et al. “Arabidopsis Thaliana Dehydroascorbate Reductase 2 : Conformational Flexibility During Catalysis.” SCIENTIFIC REPORTS 7 (2017): n. pag. Print.