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Figure 1
Overall structure of monomeric CRM197 in two views, showing its three domains with colored surfaces. The 40 primary amines (lysines plus the N-terminus) are shown as spheres. The N-terminal sphere and N-terminal catalytic domain are colored blue, the second domain is colored green and the C-terminal receptor-binding domain is colored pink. The hinge loop that connects domains 2 and 3 and that rearranges to form the dimer is shown in stick representation. The ɛ-amines of Lys385 (within the hinge) and Lys419 (behind the hinge) are colored magenta.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 79| Part 4| April 2023| Pages 82-86
https://doi.org/10.1107/S2053230X23002364
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