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

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posted on 2009-07-01, 00:00 authored by M Kurz, I Iturbe-Ormaetxe, R Jarrott, S Shouldice, Merridee Wouters, P Frei, R Glockshuber, S O’Neill, B Heras, J Martin
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.

History

Journal

Antioxidants & redox signalling

Volume

11

Pagination

1485 - 1500

Publisher

Mary Ann Liebert Publishers

Location

New Rochelle, N. Y.

ISSN

1523-0864

eISSN

1557-7716

Language

eng

Notes

Reproduced with the kind permissions of the copyright owner.

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2009, Mary Ann Liebert Publishers

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