6n04 | pdb_00006n04

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

spinqualitylabelsall models 6n04, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6n04 is a 2 chain structure with sequence from Streptomyces sp. lc-6-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. The crystal structure of AbsH3: A putative flavin adenine dinucleotide-dependent reductase in the abyssomicin biosynthesis pathway.,Clinger JA, Wang X, Cai W, Zhu Y, Miller MD, Zhan CG, Van Lanen SG, Thorson JS, Phillips GN Jr Proteins. 2020 Aug 27. doi: 10.1002/prot.25994. PMID:32852843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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