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. 2019 Apr 5;10:704. doi: 10.3389/fmicb.2019.00704

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Copyright © 2019 Wang, Guan, Zhang, Chen 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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Structural modeling and catalytic residue analysis of PB2SF. (A) Stereo view of the entire three-dimensional model. Amino acids around the active site are shown in stick mode. Notably, the Cys92 residue was not transformed to FGly in structural modeling, as it was in the active form after post-translational modification. (B) More detailed stereo view of the active site region. Figures were created with the program PyMOL. (C) Enzymatic activity analysis of PB2SF mutants. The activities of PB2SF mutants against ΔD disaccharides were measured in HAc-NaAc buffer (pH 6.0) at 40°C for 10 min. Data are shown as a percentage of the activity of wild-type PB2SF under optimal reaction conditions.