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

Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):328-333. doi: 10.1107/S2053230X21008943. Epub 2021 Sep 21.

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.

Keywords: DynU16; START/Bet v1 domain; dynemicin; helix-grip fold.

MeSH terms

  • Amino Acid Sequence
  • Anthraquinones / metabolism*
  • Anti-Bacterial Agents / biosynthesis*
  • Crystallography, X-Ray
  • Enediynes / metabolism*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Models, Molecular
  • Multigene Family
  • Protein Conformation

Substances

  • Anthraquinones
  • Anti-Bacterial Agents
  • Enediynes
  • Escherichia coli Proteins
  • dynemicin A