3I4X
Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus in complex with Trp and DMSPP
Summary for 3I4X
| Entry DOI | 10.2210/pdb3i4x/pdb |
| Related | 3I4Z |
| Descriptor | Tryptophan dimethylallyltransferase, DIMETHYLALLYL S-THIOLODIPHOSPHATE, TRYPTOPHAN, ... (5 entities in total) |
| Functional Keywords | prenyl transferase, dimethylallyl tryptophan synthase, pt barrel, tryptophan complex, dimethylallyl s-thiolodiphosphate complex, alkaloid metabolism, transferase |
| Biological source | Aspergillus fumigatus (Sartorya fumigata) |
| Total number of polymer chains | 2 |
| Total formula weight | 107101.13 |
| Authors | Schall, C.,Zocher, G.,Stehle, T. (deposition date: 2009-07-03, release date: 2009-09-01, Last modification date: 2023-11-01) |
| Primary citation | Metzger, U.,Schall, C.,Zocher, G.,Unsoeld, I.,Stec, E.,Li, S.-M.,Heide, L.,Stehle, T. The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria Proc.Natl.Acad.Sci.USA, 106:14309-14314, 2009 Cited by PubMed Abstract: Ergot alkaloids are toxins and important pharmaceuticals that are produced biotechnologically on an industrial scale. The first committed step of ergot alkaloid biosynthesis is catalyzed by dimethylallyl tryptophan synthase (DMATS; EC 2.5.1.34). Orthologs of DMATS are found in many fungal genomes. We report here the x-ray structure of DMATS, determined at a resolution of 1.76 A. A complex of DMATS from Aspergillus fumigatus with its aromatic substrate L-tryptophan and with an analogue of its isoprenoid substrate dimethylallyl diphosphate reveals the structural basis of this enzyme-catalyzed Friedel-Crafts reaction, which shows strict regiospecificity for position 4 of the indole nucleus of tryptophan as well as unusual independence of the presence of Mg(2+) ions. The 3D structure of DMATS belongs to a rare beta/alpha barrel fold, called prenyltransferase barrel, that was recently discovered in a small group of bacterial enzymes with no sequence similarity to DMATS. These bacterial enzymes catalyze the prenylation of aromatic substrates in the biosynthesis of secondary metabolites (i.e., a reaction similar to that of DMATS). PubMed: 19706516DOI: 10.1073/pnas.0904897106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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