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Figure 5
Sequence alignment showing several highly conserved residues in the MazF toxin. (a) Sequence alignment of K. pneumoniae MazF and five structural homologs. Identical and similar residues are highlighted in red and yellow, respectively. The conserved residues involved in the formation of the tertiary structure of MazF, interaction with the substrate and RNA catalysis are indicated by green squares, blue circles and red pentagrams, respectively. (b) Superimposition of the MazF monomer with its substrate-bound structural homologs. Three substrate-bound MazF toxins were used for comparison. a: Proline undergoing stacking interactions with the uracil base of the substrate. b: Arginine and threonine are highly conserved in structural homologs of MazF. c: Aspartate (glutamate) and glutamine tightly interact with adenosine and uracil via hydrogen bonding.

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