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

Alvarado, S. K.; Miller, M. D.; Bhardwaj, M.; Thorson, J. S.; Van Lanen, S. G.; Phillips, G. N.

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

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S2053230X21008943.pdf (831.35 KB)

Date

2021

Authors

Publisher

International Union of Crystallography

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.

Type

Journal article

Citation

Alvarado, S. K., Miller, M. D., Bhardwaj, M., et al.. "Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis." Acta Crystallographica Section F: Structural Biology Communications, 77, no. 10 (2021) International Union of Crystallography: 328-333. https://doi.org/10.1107/S2053230X21008943.

Published Version

https://doi.org/10.1107/S2053230X21008943

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This 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.