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==Crystal structure of Tryptophan 7-halogenase (PrnA) Mutant E450K==
==Crystal structure of Tryptophan 7-halogenase (PrnA) Mutant E450K==
<StructureSection load='4z43' size='340' side='right' caption='[[4z43]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='4z43' size='340' side='right' caption='[[4z43]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_7-halogenase Tryptophan 7-halogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.19.9 1.14.19.9] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_7-halogenase Tryptophan 7-halogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.19.9 1.14.19.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z43 OCA], [http://pdbe.org/4z43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z43 RCSB], [http://www.ebi.ac.uk/pdbsum/4z43 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z43 OCA], [http://pdbe.org/4z43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z43 RCSB], [http://www.ebi.ac.uk/pdbsum/4z43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z43 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==

Revision as of 09:09, 10 May 2017

Crystal structure of Tryptophan 7-halogenase (PrnA) Mutant E450KCrystal structure of Tryptophan 7-halogenase (PrnA) Mutant E450K

Structural highlights

4z43 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Tryptophan 7-halogenase, with EC number 1.14.19.9
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRNA_PSEFL] Involved in the biosynthesis of the antifungal antibiotic pyrrolnitrin. Catalyze the chlorination of tryptophan (Trp) at C7 position to yield 7-chloro-L-tryptophan (7-CLT). The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp.[1] [2] [3]

References

  1. ↑ Keller S, Wage T, Hohaus K, Holzer M, Eichhorn E, van Pee KH. Purification and Partial Characterization of Tryptophan 7-Halogenase (PrnA) from Pseudomonas fluorescens This work was supported by the Deutsche Forschungsgemeinschaft (DFG) through the Graduiertenkolleg "Struktur-Eigenschafts-Beziehungen bei Heterocyclen", the Environment and Climate Research and Technology Development Programme of the European Union, the Sachsische Staatsministerium fur Umwelt und Landesentwicklung, the Max-Buchner-Stiftung, and the Fonds der Chemischen Industrie. Samples of P. fluorescens BL915DeltaORF1-4 with pPEH14(prnA) and pPEH14(prnC) were obtained from Dr. J. M. Ligon, Novartis Agribusiness Biotechnology Research, Inc., Research Triangle, NC (USA) and NADH oxidase (from Thermus thermiphilus) from Prof. Helmut Erdmann, Fachhochschule Flensburg (Germany). Angew Chem Int Ed Engl. 2000 Jul 3;39(13):2300-2302. PMID:10941070
  2. ↑ Hammer PE, Hill DS, Lam ST, Van Pee KH, Ligon JM. Four genes from Pseudomonas fluorescens that encode the biosynthesis of pyrrolnitrin. Appl Environ Microbiol. 1997 Jun;63(6):2147-54. PMID:9172332
  3. ↑ Kirner S, Hammer PE, Hill DS, Altmann A, Fischer I, Weislo LJ, Lanahan M, van Pee KH, Ligon JM. Functions encoded by pyrrolnitrin biosynthetic genes from Pseudomonas fluorescens. J Bacteriol. 1998 Apr;180(7):1939-43. PMID:9537395

4z43, resolution 2.29Å

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