Structural and functional characterization of the oxidoreductase alpha-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 alpha-DsbA1 from wolbachia pipientis. Antioxidants and Redox Signaling, 11 7: 1485-1500. doi:10.1089/ars.2008.2420

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Author 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.
Title Structural and functional characterization of the oxidoreductase alpha-DsbA1 from wolbachia pipientis
Formatted title
Structural and Functional Characterization of the Oxidoreductase α-DsbA1 from Wolbachia pipientis
Journal name Antioxidants and Redox Signaling   Check publisher's open access policy
ISSN 1523-0864
1557-7716
Publication date 2009-07
Year available 2009
Sub-type Article (original research)
DOI 10.1089/ars.2008.2420
Open Access Status
Volume 11
Issue 7
Start page 1485
End page 1500
Total pages 6
Editor Chandan K. Sen
Place of publication New Rochelle, NY, U.S.A.
Publisher Mary Ann Liebert
Collection year 2010
Language eng
Subject 06 Biological Sciences
C1
920109 Infectious Diseases
970106 Expanding Knowledge in the Biological Sciences
060112 Structural Biology (incl. Macromolecular Modelling)
060107 Enzymes
060502 Infectious Agents
Formatted abstract
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.
Keyword Disulfide bond formation
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Thu, 03 Sep 2009, 08:05:19 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience