view article
Figure 3
Structural features of the MazF toxin. (a) MazF consists of seven antiparallel β-strands flanked by three α-helices. A cartoon representation of the MazF dimer (left). A topology diagram with secondary structural elements of MazF (right). (b) The residues involved in hydro­phobic interactions are shown in stick representation. A hydro­phobic core is formed around the α3-helices. (c) Superimposition of the MazF monomer with its structural homologs. Five homologs were used for comparison. The conformations of loops β1–β2, β3–β4 and β4–β5 are quite different from each other.

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