TY - JOUR
T1 - The crystal structure of AbsH3
T2 - A putative flavin adenine dinucleotide-dependent reductase in the abyssomicin biosynthesis pathway
AU - Clinger, Jonathan A.
AU - Wang, Xiachang
AU - Cai, Wenlong
AU - Zhu, Yanyan
AU - Miller, Mitchell D.
AU - Zhan, Chang Guo
AU - Van Lanen, Steven G.
AU - Thorson, Jon S.
AU - Phillips, George N.
N1 - Publisher Copyright:
© 2020 Wiley Periodicals LLC.
PY - 2021/1
Y1 - 2021/1
N2 - 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.
AB - 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.
KW - X-ray crystallography
KW - antibiotics
KW - ice rings
KW - natural product
KW - oxidoreductase
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U2 - 10.1002/prot.25994
DO - 10.1002/prot.25994
M3 - Comment/debate
C2 - 32852843
AN - SCOPUS:85093833999
SN - 0887-3585
VL - 89
SP - 132
EP - 137
JO - Proteins: Structure, Function and Bioinformatics
JF - Proteins: Structure, Function and Bioinformatics
IS - 1
ER -