Alvarado, S. K.Miller, M. D.Bhardwaj, M.Thorson, J. S.Van Lanen, S. G.Phillips, G. N.2021-10-212021-10-212021Alvarado, S. K., Miller, M. D., Bhardwaj, M., et al.. "Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis." <i>Acta Crystallographica Section F: Structural Biology Communications,</i> 77, no. 10 (2021) International Union of Crystallography: 328-333. https://doi.org/10.1107/S2053230X21008943.https://hdl.handle.net/1911/111586The 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.engThis is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.Journal articleS2053230X21008943https://doi.org/10.1107/S2053230X21008943