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Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae - a 15N -1H heteronuclear NMR relaxation analysis of oxidised and reduced forms of DsbA

Horne, James, d'Auvergne, Edward J., Coles, Murray, Velkov, Tony, Charman, William N., Prankerd, Richard, Gooley, Paul R., Scanlon, Martin J. and Chin, Yanni 2007, Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae - a 15N -1H heteronuclear NMR relaxation analysis of oxidised and reduced forms of DsbA, Journal of molecular biology, vol. 371, no. 3, pp. 703-716, doi: 10.1016/j.jmb.2007.05.067.

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Title Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae - a 15N -1H heteronuclear NMR relaxation analysis of oxidised and reduced forms of DsbA
Formatted title Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae - a 15N - 1H heteronuclear NMR relaxation analysis of oxidized and reduced forms of DsbA
Author(s) Horne, James
d'Auvergne, Edward J.
Coles, Murray
Velkov, Tony
Charman, William N.
Prankerd, Richard
Gooley, Paul R.
Scanlon, Martin J.
Chin, Yanni
Journal name Journal of molecular biology
Volume number 371
Issue number 3
Start page 703
End page 716
Publisher Academic Press
Place of publication London, England
Publication date 2007-08-17
ISSN 0022-2836
1089-8638
Keyword(s) DsbA
dynamics
bacterial oxidoreductase
model-free
interdomain motion
Summary We have determined the structure of the reduced form of the DsbA oxidoreductase from Vibrio cholerae. The reduced structure shows a high level of similarity to the crystal structure of the oxidized form and is typical of this class of enzyme containing a thioredoxin domain with an inserted α-helical domain. Proteolytic and thermal stability measurements show that the reduced form of DsbA is considerably more stable than the oxidized form. NMR relaxation data have been collected and analyzed using a model-free approach to probe the dynamics of the reduced and oxidized states of DsbA. Akaike's information criteria have been applied both in the selection of the model-free models and the diffusion tensors that describe the global motions of each redox form. Analysis of the dynamics reveals that the oxidized protein shows increased disorder on the pico- to nanosecond and micro- to millisecond timescale. Many significant changes in dynamics are located either close to the active site or at the insertion points between the domains. In addition, analysis of the diffusion data shows there is a clear difference in the degree of interdomain movement between oxidized and reduced DsbA with the oxidized form being the more rigid. Principal components analysis has been employed to indicate possible concerted movements in the DsbA structure, which suggests that the modeled interdomain motions affect the catalytic cleft of the enzyme. Taken together, these data provide compelling evidence of a role for dynamics in the catalytic cycle of DsbA.
Language eng
DOI 10.1016/j.jmb.2007.05.067
Field of Research 060107 Enzymes
030402 Biomolecular Modelling and Design
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2007, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30019302

Document type: Journal Article
Collection: School of Medicine
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