5Z44
Crystal structure of prenyltransferase AmbP1 complexed with GSPP
Summary for 5Z44
| Entry DOI | 10.2210/pdb5z44/pdb |
| Descriptor | AmbP1, GERANYL S-THIOLODIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | prenyltransferase, ambp1, indole, transferase |
| Biological source | Fischerella ambigua UTEX 1903 |
| Total number of polymer chains | 2 |
| Total formula weight | 71018.53 |
| Authors | Awakawa, T.,Nakashima, Y.,Mori, T.,Abe, I. (deposition date: 2018-01-10, release date: 2018-06-06, Last modification date: 2025-09-17) |
| 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 Cited by 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: 29677386DOI: 10.1002/anie.201800855 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.458 Å) |
Structure validation
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