Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis.

ABSTRACT: The 1.5 Å resolution crystal structure of DynU16, a protein identified in the dynemicin-biosynthetic gene cluster, is reported. The structure adopts a di-domain helix-grip fold with a uniquely positioned open cavity connecting the domains. The elongated dimensions of the cavity appear to be compatible with the geometry of a linear polyene, suggesting the involvement of DynU16 in the upstream steps of dynemicin biosynthesis.

SUBMITTER: Alvarado SK 

PROVIDER: S-EPMC8488855 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature