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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

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

Alvarado Sarah K SK Miller Mitchell D MD Bhardwaj Minakshi M Thorson Jon S JS Van Lanen Steven G SG Phillips George N GN

Acta crystallographica. Section F, Structural biology communications 20210921 Pt 10

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. ...[more]

PMID: 34605436

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