Molecular Insight into the Mg2+ -Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1.
Angew Chem Int Ed Engl
; 57(23): 6810-6813, 2018 06 04.
Article
in En
| MEDLINE
| ID: mdl-29677386
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 (Mg2+ ) 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 Mg2+ effector. The comparative study of these structures revealed a unique allosteric binding site for Mg2+ 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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Cyanobacteria
/
Dimethylallyltranstransferase
/
Indoles
/
Magnesium
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2018
Document type:
Article
Affiliation country:
Japan