5Y4G

Apo Structure of AmbP3

Summary for 5Y4G

• Entry DOI: 10.2210/pdb5y4g/pdb
• Descriptor: AmbP3 (2 entities in total)
• Functional Keywords: prenyltransferase, transferase
• Biological source: Fischerella ambigua UTEX 1903
• Total number of polymer chains: 2
• Total formula weight: 76088.23

Authors

Wong, C.P.,Awakawa, T.,Nakashima, Y. (deposition date: 2017-08-03, release date: 2018-07-18, Last modification date: 2024-03-27)

Primary citation

Wong, C.P.,Awakawa, T.,Nakashima, Y.,Mori, T.,Zhu, Q.,Liu, X.,Abe, I.
Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3
Angew. Chem. Int. Ed. Engl., 57:560-563, 2018

PubMed Abstract: 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 Å 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.

PubMed: 29178634
DOI: 10.1002/anie.201710682

Experimental method

X-RAY DIFFRACTION (2 Å)