The crystal structure of AbsH3: A putative flavin adenine dinucleotide-dependent reductase in the abyssomicin biosynthesis pathway

Jonathan A. Clinger, Xiachang Wang, Wenlong Cai, Yanyan Zhu, Mitchell D. Miller, Chang Guo Zhan, Steven G. Van Lanen, Jon S. Thorson, George N. Phillips

Research output: Contribution to journalComment/debate

1 Scopus citations

Abstract

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 in Streptomyces sp. LC-6-2.

Original languageEnglish
Pages (from-to)132-137
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Volume89
Issue number1
DOIs
StatePublished - Jan 2021

Bibliographical note

Publisher Copyright:
© 2020 Wiley Periodicals LLC.

Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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