Researchers are exploring whether these ubiquitous fluorinated molecules might worsen infections or hamper vaccine effectiveness.
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Edited by Arnold L. Demain, Drew University, Madison, NJ, and approved July 9, 2009
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↵1U.M. and C.S. contributed equally to this work. (received for review May 5, 2009)
Article Figures & SI
Figures
- Fig. 1.
Reaction catalyzed by DMATS, and structures of ergot alkaloids.
- Fig. 2.
Stereo drawing showing the 3D architecture of FgaPT2. The structure is shown as a ribbon drawing, with the 10 β-strands colored yellow and the remaining residues colored green. The ligands L-tryptophan and DMSPP as well as residues that contact them via hydrogen bonds or salt bridges are shown as ball-and-stick models, with the following color code: nitrogen, blue; oxygen, red; phosphate, gray, and sulfur, yellow. Carbon atoms are green (FgaPT2), blue (L-tryptophan), and orange (DMSPP). Hydrogen bonds and salt bridges between protein and ligand atoms are represented with dashed red lines. Secondary structure elements are numbered. N and C denote the N-terminus and C-terminus, respectively.
- Fig. 3.
Active center of FgaPT2 and comparison with the NphB active site. (A) View of the DMSPP in the active site of FgaPT2. Side chains binding the pyrophosphate are shown. (B) View of the active site of NphB. Side chains binding the pyrophosphate are shown. (C) View of the residues in the active site of FgaPT2 forming the binding pocket for L-tryptophan and the dimethylallyl chain of DMSPP. (D) Active site residues in liganded and unliganded (gray) FgaPT2 undergoing conformational changes upon ligand binding. Dashed red lines show contacts/hydrogen bonds with less than 3.2 Å.
- Fig. 4.
Hypothetical reaction mechanism for DMATS.
Data supplements
Supporting Information
Files in this Data Supplement:
The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria
Article Classifications
- Biological Sciences
- Biochemistry
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