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Figure 4
A structural study based on electronic surface potential. (a) Comparison of antitoxin-bound MazF with substrate-bound MazF via electronic surface potential. MazF-dimer transition between the open and closed states in the TA interface pocket through conformational change of loop β1–β2. Site A (yellow oval): the specific binding pocket of the downstream region of the RNA substrate. RBP (gray oval): the specific binding pocket of the upstream region of the RNA substrate. (b) Opposite electrostatic surface potential in TA interface pockets between K. pneumoniae MazEF and M. tuberculosis MazEF4. The electrostatic surface potential of MazF toxin along with cartoon representations of K. pneumoniae MazE (wheat) and M. tuberculosis MazE (light blue) (upper). The electrostatic surface potential of the C terminus of K. pneumoniae MazE and M. tuberculosis MazE4 along with cartoon representations of K. pneumoniae MazF (chain E: blue, chain F: green) and M. tuberculosis MazF (chain A: orange, chain B: brown) (lower). The TA interface pocket and charged MazF-binding patches are marked.

IUCrJ
Volume 8| Part 3| May 2021| Pages 362-371
ISSN: 2052-2525
https://doi.org/10.1107/S2052252521000452