view article

Figure 4
The importance of the zinc-finger domain for abTrx2 activity. (a) Sequence alignment of Trx2 from different species (ab: A. baumannii; rc: R. capsulatus; yp: Y. pestis; ec: E. coli; dr: D. radiodurans). The CxxC motif is enclosed in a black-dotted box. The four cysteine residues involved in zinc ion coordination are indicated by asterisks (*). Completely and partially conserved residues across the different species are shown in red and blue, respectively. (b) A graphic representation of abTrx2 colored according to the degree of amino acid sequence conservation generated by the ConSurf server. (c) A cartoon figure showing the hydrogen bonds mediated by Asn12 in the zinc-finger fold of abTrx2. (d) A cartoon figure showing the hydrogen bonds mediated by conserved Asn12 (Asn22 of rcTrx2 and Asn12 of ypTrx2) in the zinc-finger fold. (e) abTrx2 mutant activity analysis by DTNB reduction assay. The reduction of DTNB by abTrxR was tested in the presence of abTrx2 mutants. Error bars indicate the standard deviation for three independent experiments (n = 3).

Volume 10| Part 2| March 2023| Pages 147-155
ISSN: 2052-2525