View source for 6frl


==BrvH, a flavin-dependent halogenase from Brevundimonas sp. BAL3==
<StructureSection load='6frl' size='340' side='right' caption='[[6frl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6frl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FRL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FRL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=6frl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6frl OCA], [http://pdbe.org/6frl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6frl RCSB], [http://www.ebi.ac.uk/pdbsum/6frl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6frl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavin-dependent halogenases catalyse halogenation of aromatic compounds. In most cases, this reaction proceeds with high regioselectivity and requires only the presence of FADH2, oxygen, and halide salts. Since marine habitats contain high concentrations of halides, organisms populating the oceans might be valuable sources of yet undiscovered halogenases. A new Hidden-Markov-Model (HMM) based on the PFAM tryptophan halogenase model was used for the analysis of marine metagenomes. Eleven metagenomes were screened leading to the identification of 254 complete or partial putative flavin-dependent halogenase genes. One predicted halogenase gene (brvH) was selected, codon optimised for E. coli, and overexpressed. Substrate screening revealed that this enzyme represents an active flavin-dependent halogenase able to convert indole to 3-bromoindole. Remarkably, bromination prevails also in a large excess of chloride. The BrvH crystal structure is very similar to that of tryptophan halogenases but reveals a substrate binding site that is open to the solvent instead of being covered by a loop.

A flavin-dependent halogenase from metagenomic analysis prefers bromination over chlorination.,Neubauer PR, Widmann C, Wibberg D, Schroder L, Frese M, Kottke T, Kalinowski J, Niemann HH, Sewald N PLoS One. 2018 May 10;13(5):e0196797. doi: 10.1371/journal.pone.0196797., eCollection 2018. PMID:29746521<ref>PMID:29746521</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6frl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Neubauer, P R]]
[[Category: Niemann, H H]]
[[Category: Sewald, N]]
[[Category: Widmann, C]]
[[Category: Flavin-dependent halogenase]]
[[Category: Flavoprotein]]