Conformational changes and subunit communication in tryptophan synthase: effect of substrates and substrate analogs

A study was conducted on regulatory signal communication and conformational changes in alpha- and beta- subunits of the tryptophan synthase alpha2beta2 complex from Salmonella typhimurium. Results showed that the binding of DL-alpha-glycerol 3-phosphate influences the structure of the alpha-subunit and promotes conformational change leading to structural rigidity in the beta-subunit in the presence of coenzyme. The mechanisms and implications of allosteric regulation between alpha- and beta- subunits are also presented.