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. Author manuscript; available in PMC: 2020 Sep 10.
Published in final edited form as: Chem Commun (Camb). 2019 Sep 10;55(73):10844–10847. doi: 10.1039/c9cc05936a

Figure 1:

Figure 1:

(A) PaZntA51–740 3D homology model based on the A. Fulgidus CopA cryo-EM model (PDB 3J09, which include the N-terminal MBD) and (B) close-up view of the expected high-affinity TM-MBS. Cys391, Cys393 and Asp721 (conserved in ZntAs) are responsible for transmembrane substrate binding, while Lys700 on M6 acts as a built-in counterion. A similar model was also obtained based on the structure of S. Sonnei ZntA (PDB 3J09). (C) Relative ATPase activity of PaΔZntA121–740 in proteoliposomes as a function of different metals (40 µM, see Material and Methods; Zn(II)-ATPase activity ∼ 0.9 nmol/(mg·min) ) and (D) the influence of P-type ATPases inhibitors (VO43-, AlF4-, ouabain) and non-hydrolysable nucleotide analogues (AMPPCP).