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.
|Number of pages||6|
|Journal||Acta Crystallographica Section F:Structural Biology Communications|
|State||Published - Oct 1 2021|
Bibliographical noteFunding Information:
Funding for this research was provided by: National Institutes of Health, National Institute of General Medical Sciences (grant No. GM115261 to George N. Phillips Jr, Jon S. Thorson; studentship No. T32GM0082280 to Sarah K. Alvarado); National Institutes of Health, National Cancer Institute (grant No. CA217255 to George N. Phillips Jr, Jon S. Thorson, Steven G. Van Lanen); National Science Foundation, BioXFEL Science and Technology Center (grant No. 1231306 to George N. Phillips Jr).
This work used research resources provided by the University of Kentucky Center of Biomedical Research Excellence (COBRE) in Pharmaceutical Research and Innovation (CPRI; NIH P20 GM130456), College of Pharmacy and the National Center for Advancing Translational Sciences (UL1TR000117 and UL1TR001998). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health or the National Science Foundation.
© 2021 International Union of Crystallography. All rights reserved.
- Helix-grip fold
- START/Bet v1 domain
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics