6N04

The X-ray crystal structure of AbsH3, an FAD dependent reductase from the Abyssomicin biosynthesis pathway in Streptomyces

Summary for 6N04

• Entry DOI: 10.2210/pdb6n04/pdb
• Descriptor: AbsH3, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, biosynthesis, abyssomicin, structural genomics, psi-biology, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, biosynthetic protein
• Biological source: Streptomyces sp. LC-6-2
• Total number of polymer chains: 2
• Total formula weight: 93823.35

Authors

Clinger, J.A.,Wang, X.,Cai, W.,Miller, M.D.,Van Lanen, S.G.,Thorson, J.S.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2018-11-06, release date: 2019-11-13, Last modification date: 2023-10-11)

Primary citation

Clinger, J.A.,Wang, X.,Cai, W.,Zhu, Y.,Miller, M.D.,Zhan, C.G.,Van Lanen, S.G.,Thorson, J.S.,Phillips Jr., G.N.
The crystal structure of AbsH3: A putative flavin adenine dinucleotide-dependent reductase in the abyssomicin biosynthesis pathway.
Proteins, 2020

PubMed 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.

PubMed: 32852843
DOI: 10.1002/prot.25994

Experimental method

X-RAY DIFFRACTION (1.998 Å)