Structural design principles for specific ultra-high affinity interactions between colicins/pyocins and immunity proteins.

ABSTRACT: The interactions of the antibiotic proteins colicins/pyocins with immunity proteins is a seminal model system for studying protein-protein interactions and specificity. Yet, a precise and quantitative determination of which structural elements and residues determine their binding affinity and specificity is still lacking. Here, we used comparative structure-based energy calculations to map residues that substantially contribute to interactions across native and engineered complexes of colicins/pyocins and immunity proteins. We show that the immunity protein α1-α2 motif is a unique structurally-dissimilar element that restricts interaction specificity towards all colicins/pyocins, in both engineered and native complexes. This motif combines with a diverse and extensive array of electrostati

SUBMITTER: Shushan A 

PROVIDER: S-EPMC7884437 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature