Bidirectional interdomain crosstalk in a <i>Porphyromonas gingivalis</i> chimeric enzyme coordinates catalytic synergy for aromatic amino acid biosynthesis.

ABSTRACT: The shikimate pathway, critical for bacterial aromatic amino acid biosynthesis, represents a prime therapeutic target due to its absence in humans. This study elucidates the structural and functional interplay within the bifunctional enzyme DAH7PS-CM from Porphyromonas gingivalis (PgiDAH7PS-CM), a keystone periodontal pathogen. Integrating AlphaFold3-predicted models with biochemical validation, we identified two interdomain interfaces: a conserved DAH7PS dimerization interface and a polar interaction-driven D-CM interface (e.g., E287/R291). Mutagenesis of these residues and exposure to high Na⁺ concentrations disrupted enzyme function, confirming polar networks mediate domain crosstalk. The DAH7PS domain's dimerization relies on conserved interfaces homologous to

SUBMITTER: Yu Y 

PROVIDER: S-EPMC12202928 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature