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

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 compatib...

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Detalles Bibliográficos
Autores principales: Alvarado, Sarah K., Miller, Mitchell D., Bhardwaj, Minakshi, Thorson, Jon S., Van Lanen, Steven G., Phillips, George N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8488855/
https://www.ncbi.nlm.nih.gov/pubmed/34605436
http://dx.doi.org/10.1107/S2053230X21008943
Descripción
Sumario: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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