6V04

DynU16 crystal structure, a putative protein in the dynemicin biosynthetic locus

Summary for 6V04

Entry DOI	10.2210/pdb6v04/pdb
Descriptor	Uncharacterized SRPBCC domain-containing protein, SODIUM ION, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	dynemicin, start domain, srpbcc domain, cyclase/aromatase, unknown function
Biological source	Micromonospora chersina
Total number of polymer chains	1
Total formula weight	32089.38
Authors	Alvarado, S.K.,Miller, M.D.,Bhardwaj, M.,Thorson, J.S.,Van Lanen, S.G.,Phillips Jr., G.N. (deposition date: 2019-11-18, release date: 2020-11-18, Last modification date: 2024-05-22)
Primary citation	Alvarado, S.K.,Miller, M.D.,Bhardwaj, M.,Thorson, J.S.,Van Lanen, S.G.,Phillips Jr., G.N. Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis. Acta Crystallogr.,Sect.F, 77:328-333, 2021 Cited by PubMed 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. PubMed: 34605436 DOI: 10.1107/S2053230X21008943 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation