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Updated: Oct 18, 2025

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028
Published on: January 13, 2017
Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
Sarah K Alvarado1, Mitchell D Miller1, Minakshi Bhardwaj2
1Department of BioSciences, Rice University, 6100 Main Street, Houston, TX 77005, USA.
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.
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