2ard | pdb_00002ard
The structure of tryptophan 7-halogenase (PrnA) suggests a mechanism for regioselective chlorination
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Overview
Chlorinated natural products include vancomycin and cryptophycin A. Their, biosynthesis involves regioselective chlorination by flavin-dependent, halogenases. We report the structural characterization of tryptophan, 7-halogenase (PrnA), which regioselectively chlorinates tryptophan., Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10, angstrom-long tunnel and bound by distinct enzyme modules. The FAD module, is conserved in halogenases and is related to flavin-dependent, monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2, to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is, guided through the tunnel to tryptophan, where it is activated to, participate in electrophilic aromatic substitution.
About this Structure
2ARD is a Single protein structure of sequence from Pseudomonas fluorescens with FDA as ligand. Full crystallographic information is available from OCA.
Reference
Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination., Dong C, Flecks S, Unversucht S, Haupt C, van Pee KH, Naismith JH, Science. 2005 Sep 30;309(5744):2216-9. PMID:16195462
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Pseudomonas fluorescens
- Single protein
- Dong, C.
- Flecks, S.
- Haupt, C.
- Naismith, J.H.
- Pee, K.H.Van.
- SSPF, Scottish.Structural.Proteomics.Facility.
- Unversucht, S.
- FDA
- Flavin-dependent halogenase
- Helical bundle
- Sandwiched sheets
- Scottish structural proteomics facility
- Sspf
- Structural genomics
- Tryptophan 7-halogenase
