Structural highlights
Function
B2BM46_9ACTN
Publication Abstract from PubMed
The 1.5 A 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.
Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis.,Alvarado SK, Miller MD, Bhardwaj M, Thorson JS, Van Lanen SG, Phillips GN Jr Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):328-333. doi:, 10.1107/S2053230X21008943. Epub 2021 Sep 21. PMID:34605436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alvarado SK, Miller MD, Bhardwaj M, Thorson JS, Van Lanen SG, Phillips GN Jr. Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis. Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):328-333. doi:, 10.1107/S2053230X21008943. Epub 2021 Sep 21. PMID:34605436 doi:http://dx.doi.org/10.1107/S2053230X21008943