PDBsum entry: 3i4x

Transferase

PDB id: 3i4x

Contents

Protein chains

428 a.a. *

Ligands

DST ×2

TRP ×2

GOL ×2

Waters ×585

* Residue conservation analysis

PDB id:

3i4x

Name:

Transferase

Title:

Crystal structure of the dimethylallyl tryptophan synthase f aspergillus fumigatus in complex with trp and dmspp

Structure:

Tryptophan dimethylallyltransferase. Chain: a, b. Synonym: l-tryptophan dimethylallyl transferase, dmats, all hexaprenyl-diphosphate synthase. Engineered: yes

Source:

Aspergillus fumigatus. Sartorya fumigata. Organism_taxid: 5085. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.151 R-free: 0.200

Authors:

C.Schall,G.Zocher,T.Stehle

Key ref:

U.Metzger et al. (2009). The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria. Proc Natl Acad Sci U S A, 106, 14309-14314. PubMed id: 19706516

Date:

03-Jul-09 Release date: 01-Sep-09

Protein chains

Q50EL0  (DMAW_ASPFU) -  Tryptophan dimethylallyltransferase

Seq: 459 a.a.

Struc: 428 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.5.1.34 - 4-dimethylallyltryptophan synthase.
• Reaction: Dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut- 2-enyl)-L-tryptophan

Dimethylallyl diphosphate + L-tryptophan (Bound ligand (Het Group name = TRP) corresponds exactly) = diphosphate (Bound ligand (Het Group name = DST) matches with 53.33% similarity) + 4-(3-methylbut- 2-enyl)-L-tryptophan

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: alkaloid metabolic process (1 term)
• Biochemical function: transferase activity (2 terms)

reference

Proc Natl Acad Sci U S A 106:14309-14314 (2009)

PubMed id: 19706516

The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.

U.Metzger, C.Schall, G.Zocher, I.Unsöld, E.Stec, S.M.Li, L.Heide, T.Stehle.

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).