Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family

ABSTRACT: The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures as well as enzymological data demonstrate that a conserved tetramer interface maintains the active site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an equivalent active site structure in the context of a single subunit. Oligomerization therefore enhances evolutionary fitness by reducing the metabolic cost of enzyme biosynthesis. The large surface area of the structure-stabilizing oligomeric interface yields a synergistic gain in fitness by inc

SUBMITTER: Yaohui Li 

PROVIDER: S-SCDT-EMBOJ-2021-108368 | biostudies-other |

REPOSITORIES: biostudies-other