5YK9

Crystal structure of selenomethionine-labelled indole prenyltransferase AmbP1

Summary for 5YK9

• Entry DOI: 10.2210/pdb5yk9/pdb
• Descriptor: AmbP1 (1 entity in total)
• Functional Keywords: cyanobacteria, transferase
• Biological source: Fischerella ambigua UTEX 1903
• Total number of polymer chains: 2
• Total formula weight: 70684.52

Authors

Awakawa, T.,Nakashima, Y.,Liu, X.,Abe, I. (deposition date: 2017-10-12, release date: 2018-06-06, Last modification date: 2024-10-23)

Primary citation

Awakawa, T.,Mori, T.,Nakashima, Y.,Zhai, R.,Wong, C.P.,Hillwig, M.L.,Liu, X.,Abe, I.
Molecular Insight into the Mg2+-Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1
Angew. Chem. Int. Ed. Engl., 57:6810-6813, 2018

PubMed Abstract: AmbP1 is a cyanobacterial aromatic prenyltransferase and a dedicated synthase for (R)-3-geranyl-3-isocyanovinyl indolenine (2), the biogenetic precursor for hapalindole-type alkaloids. The regioselective geranylation of cis-indolyl vinyl isonitrile (1) by the standalone AmbP1 to give 2 has been shown to require a magnesium ion (Mg ) to suppress the formation of cis-2-geranylindolyl vinyl isonitrile (3). Here, we report high-resolution crystal structures of AmbP1 in complex with 1 and geranyl S-thiodiphosphate (GSPP) in the presence and absence of a Mg effector. The comparative study of these structures revealed a unique allosteric binding site for Mg that modulates the conformation of 1 in the active site of AmbP1 for its selective geranylation. This work defines the structural basis for AmbP1 catalysis in the biogenesis of hapalindole-type alkaloids and provides the first atomic-level insight to the allosteric regulation of prenyltransferases.

PubMed: 29677386
DOI: 10.1002/anie.201800855

Experimental method

X-RAY DIFFRACTION (3.001 Å)