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dc.contributor.authorKurz, Mareike
dc.contributor.authorIturbe-Ormaetxe, Inaki
dc.contributor.authorJarrott, Russell
dc.contributor.authorShouldice, Stephen R
dc.contributor.authorWouters, Merridee A
dc.contributor.authorFrei, Patrick
dc.contributor.authorGlockshuber, Rudi
dc.contributor.authorO'Neill, Scott L
dc.contributor.authorHeras, Begona
dc.contributor.authorMartin, Jennifer L
dc.date.accessioned2017-09-22T02:19:37Z
dc.date.available2017-09-22T02:19:37Z
dc.date.issued2009
dc.identifier.issn1523-0864
dc.identifier.doi10.1089/ars.2008.2420
dc.identifier.urihttp://hdl.handle.net/10072/347139
dc.description.abstractThe 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.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherMary Ann Liebert
dc.relation.ispartofpagefrom1485
dc.relation.ispartofpageto1500
dc.relation.ispartofissue7
dc.relation.ispartofjournalAntioxidants & Redox Signaling
dc.relation.ispartofvolume11
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchMedical biochemistry and metabolomics
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode3205
dc.subject.fieldofresearchcode3214
dc.titleStructural and functional characterization of the oxidoreductase a-DsbA1 from Wolbachia pipientis
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer
gro.griffith.authorJarrott, Russell J.


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