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.
Original language | English |
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Pages (from-to) | 328-333 |
Number of pages | 6 |
Journal | Acta Crystallographica Section F:Structural Biology Communications |
Volume | 77 |
DOIs | |
State | Published - Oct 1 2021 |
Bibliographical note
Publisher Copyright:© 2021 International Union of Crystallography. All rights reserved.
Keywords
- DynU16
- Dynemicin
- Helix-grip fold
- START/Bet v1 domain
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics