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Figure 1
The crystal structure of abTrx2. (a) An overview of the function of Trx2 in the Trx redox system of A. baumannii. (b) Domain composition of Trx2 and Trx1. (c) A profile of the SEC performed to purify abTrx2. The eluted positions of standard size markers are shown above the profile. The SDS–PAGE gel loaded with the peak fractions is provided to the left of the main peak. Loaded fractions corresponding to the bands on the SDS–PAGE gel are indicated by black arrows. M and B indicate the size marker and sample before SEC, respectively. (d) A cartoon representation of abTrx2. A rainbow color scheme was used for tracing the path from N- to C-terminus. Helices and sheets are labeled with α and β, respectively. (e) A cartoon representation showing the domain structure of abTrx2. The black-dotted and red-dotted boxes indicate the CxxC redox center and zinc-binding site that are magnified in panels (f) and (g), respectively. (f) A 2Fo − Fc electron-density map contoured at the 1σ level around the CxxC redox center. Residues forming the CxxC redox center are labeled. (g) A 2Fo − Fc electron-density map contoured at the 1σ level around the zinc-binding site. The cysteine residues involved in zinc coordination are labeled. (h) A putty representation of abTrx2 showing the B-factor distribution. Rainbow colors range from red to violet to reflect B-factor values for B-factor visualization. Higher B-factor regions are indicated by black arrows.

IUCrJ
Volume 10| Part 2| March 2023| Pages 147-155
ISSN: 2052-2525
https://doi.org/10.1107/S2052252523000404