4lu6
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lu6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LU6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lu6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LU6 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu6 OCA], [https://pdbe.org/4lu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lu6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lu6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu6 OCA], [https://pdbe.org/4lu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lu6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lu6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/REBH_LENAE REBH_LENAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. 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.<ref>PMID:11983340</ref> <ref>PMID:15743914</ref> <ref>PMID:17260957</ref> | [https://www.uniprot.org/uniprot/REBH_LENAE REBH_LENAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. 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.<ref>PMID:11983340</ref> <ref>PMID:15743914</ref> <ref>PMID:17260957</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We previously reported that the halogenase RebH catalyzes selective halogenation of several heterocycles and carbocycles, but product yields were limited by enzyme instability. Here, we use directed evolution to engineer an RebH variant, 3-LR, with a Topt over 5 degrees C higher than that of wild-type, and 3-LSR, with a Tm 18 degrees C higher than that of wild-type. These enzymes provided significantly improved conversion (up to fourfold) for halogenation of tryptophan and several non-natural substrates. This initial evolution of RebH not only provides improved enzymes for immediate synthetic applications, but also establishes a robust protocol for further halogenase evolution. | ||
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| - | Improving the Stability and Catalyst Lifetime of the Halogenase RebH By Directed Evolution.,Poor CB, Andorfer MC, Lewis JC Chembiochem. 2014 May 21. doi: 10.1002/cbic.201300780. PMID:24849696<ref>PMID:24849696</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lu6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Thermostabilized RebH
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