4.3 Article

The crystal structure ofAbsH3: A putative flavin adenine dinucleotide-dependent reductase in the abyssomicin biosynthesis pathway

Journal

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 89, Issue 1, Pages 132-137

Publisher

WILEY
DOI: 10.1002/prot.25994

Keywords

antibiotics; ice rings; natural product; oxidoreductase; X-ray crystallography

Funding

  1. National Cancer Institute [CA217255]
  2. National Center for Advancing Translational Sciences [ULITR000117, ULITR001998]
  3. National Institute of General Medical Sciences [GM098248, P20-GM130456, R01GM115261, T323GM008280]
  4. United States Department of Energy [DE-AC02-06CH11357]

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Abyssomicins are natural product molecules with antibiotic activity by inhibiting the folate synthesis pathway in microbiota, and they undergo a necessary [4 + 2] cycloaddition. The structure of a flavin adenine dinucleotide-dependent reductase, AbsH3, from the biosynthetic gene cluster of novel abyssomicins found in Streptomyces sp. LC-6-2 has been reported.
Natural products and natural product-derived compounds have been widely used for pharmaceuticals for many years, and the search for new natural products that may have interesting activity is ongoing. Abyssomicins are natural product molecules that have antibiotic activity via inhibition of the folate synthesis pathway in microbiota. These compounds also appear to undergo a required [4 + 2] cycloaddition in their biosynthetic pathway. Here we report the structure of an flavin adenine dinucleotide-dependent reductase, AbsH3, from the biosynthetic gene cluster of novel abyssomicins found inStreptomycessp. LC-6-2.

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