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Structural and functional characterization of the oxidoreductase a-DsbA1 from wolbachia pipientis

Kurz, Mareike, Iturbe-Ormaetxe, Iñaki, Jarrott, Russell, Shouldice, Stephen R., Wouters, Merridee A., Frei, Patrick, Glockshuber, Rudi, O’Neill, Scott L., Heras, Begoña and Martin, Jennifer L. 2009, Structural and functional characterization of the oxidoreductase a-DsbA1 from wolbachia pipientis, Antioxidants & redox signalling, vol. 11, pp. 1485-1500, doi: 10.1089/ars.2008.2420..

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Title Structural and functional characterization of the oxidoreductase a-DsbA1 from wolbachia pipientis
Author(s) Kurz, Mareike
Iturbe-Ormaetxe, Iñaki
Jarrott, Russell
Shouldice, Stephen R.
Wouters, Merridee A.
Frei, Patrick
Glockshuber, Rudi
O’Neill, Scott L.
Heras, Begoña
Martin, Jennifer L.
Journal name Antioxidants & redox signalling
Volume number 11
Start page 1485
End page 1500
Total pages 16
Publisher Mary Ann Liebert Publishers
Place of publication New Rochelle, N. Y.
Publication date 2009-07
ISSN 1523-0864
1557-7716
Summary The α-proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host's reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable the development of inhibitors for chemical genetics studies. Wolbachia encodes a homologue (α-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA, essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia α-DsbA1 has the most reducing redox potential of any characterized DsbA. In addition, Wolbachia α-DsbA1 possesses a second disulfide that is highly conserved in α-proteobacterial DsbAs but not in other DsbAs. The α-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA, and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of α-DsbA1 indicate that it probably plays a specialized oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies.
Notes Reproduced with the kind permissions of the copyright owner.
Language eng
DOI 10.1089/ars.2008.2420.
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2009, Mary Ann Liebert Publishers
Persistent URL http://hdl.handle.net/10536/DRO/DU:30038982

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.