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Fig. 1 | Microbial Cell Factories

Fig. 1

From: Characterization of a promiscuous cadmium and arsenic resistance mechanism in Thermus thermophilus HB27 and potential application of a novel bioreporter system

Fig. 1

a Primary structure of TtArsX. Aminoacids that are predicted to be in β-turns are colored green, those in α-helices are red and those in turns are colored black. Aminoacids in orange are included in TM helices. The residues conserved in P-type ATPases are shown in bold, those which are signatures of the P1b-2 type subfamily are underlined. The CXXC motif at the N-terminus is boxed. b Schematic topology of TtArsX (adapted from [7]). MBD: soluble N-terminal metal-binding domain (hexagon); AD: actuator domain (ellipse), ATPBD: ATP binding domain. Invariant motifs in ATPBD and AD domains of P-type ATPases are shown in bold. Residues indicated in the TM helices 4,5,6 are those conserved in P1b-2 type subfamily. c 3D model of TtArsX MBD (corresponding to residue 1–91 from the intact protein) interacting with As(III), (colored blue, left) and Cd(II) (magenta, right)

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