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. 2021 Sep 24;12:735793. doi: 10.3389/fmicb.2021.735793

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Copyright © 2021 Wang, Zhang, Teng, Wang, Zhang, Chen, Zhang, Chen, Fu and Li.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The binding of the NADP⁺ molecule and the FAD molecule in Tmm₇₂₁₁. The NADP⁺ molecule and the FAD molecule are shown as sticks colored in green and yellow, respectively. (A) Electrostatic surface of Tmm₇₂₁₁. The NADP⁺ molecule is partially visible through the surface. (B) Electrostatic surface of Tmm₇₂₁₁ after the transparency of surface was set to 40%. (C) Interactions between NADP⁺ and Tmm₇₂₁₁ residues. (D) Interactions between FAD and Tmm₇₂₁₁ residues. Water molecules are shown in red dots. The possible hydrogen bonds are represented by dashed lines. (E) The enzymatic activities of WT Tmm₇₂₁₁ and its mutants. The activity of WT Tmm₇₂₁₁ is taken as 100%. The standard errors are from three independent experiments. (F) CD spectra of WT Tmm₇₂₁₁ and its mutants.