3D domain swapping in the TIM barrel of the α subunit of Streptococcus pneumoniae tryptophan synthase.

ABSTRACT: Tryptophan synthase catalyzes the last two steps of tryptophan biosynthesis in plants, fungi and bacteria. It consists of two protein chains, designated α and β, encoded by trpA and trpB genes, that function as an αββα complex. Structural and functional features of tryptophan synthase have been extensively studied, explaining the roles of individual residues in the two active sites in catalysis and allosteric regulation. TrpA serves as a model for protein-folding studies. In 1969, Jackson and Yanofsky observed that the typically monomeric TrpA forms a small population of dimers. Dimerization was postulated to take place through an exchange of structural elements of the monomeric chains, a phenomenon later termed 3D domain swapping. The structural details of the TrpA dimer have remained unk

SUBMITTER: Michalska K 

PROVIDER: S-EPMC7008512 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature