5y7c

Hapalindole A and DMSPP Bound AmbP3

spinqualitylabelsall models 5y7c, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y7c is a 2 chain structure with sequence from Fischerella ambigua UTEX 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.003Å Ligands: 8O0, DST Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V5TDY7_FISAU Publication Abstract from PubMed The cyanobacterial prenyltransferase AmbP3 catalyzes the reverse prenylation of the tetracyclic indole alkaloid hapalindole U at its C-2 position. Interestingly, AmbP3 also accepts hapalindole A, a halogenated C-10 epimer of hapalindole U, and catalyzes normal prenylation at its C-2 position. The comparison of the two ternary crystal structures, AmbP3-DMSPP/hapalindole U and AmbP3-DMSPP/hapalindole A, at 1.65-2.00 A resolution revealed two distinct orientations for the substrate binding that define reverse or normal prenylation. The tolerance of the enzyme for these altered orientations is attributed to the hydrophobicity of the substrate binding pocket and the plasticity of the amino acids surrounding the allyl group of the prenyl donor. This is the first study to provide the intimate structural basis for the normal and reverse prenylations catalyzed by a single enzyme, and it offers novel insight into the engineered biosynthesis of prenylated natural products. Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3.,Wong CP, Awakawa T, Nakashima Y, Mori T, Zhu Q, Liu X, Abe I Angew Chem Int Ed Engl. 2018 Jan 8;57(2):560-563. doi: 10.1002/anie.201710682., Epub 2017 Dec 15. PMID:29178634 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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