Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains.

ABSTRACT: Homomers are prevalent in bacterial proteomes, particularly among core metabolic enzymes. Homomerization is often key to function and regulation, and interfaces that facilitate the formation of homomeric enzymes are subject to intense evolutionary change. However, our understanding of the molecular mechanisms that drive evolutionary variation in homomeric complexes is still lacking. How is the diversification of protein interfaces linked to variation in functional regulation and structural integrity of homomeric complexes? To address this question, we studied quaternary structure evolution of bacterial methionine S-adenosyltransferases (MATs)-dihedral homotetramers formed along a large and conserved dimeric interface harboring two active sites, and a small, recently evolved, interdimeric i

SUBMITTER: Kleiner D 

PROVIDER: S-EPMC9202080 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature