4lu6: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Thermostabilized RebH==

== Structural highlights ==

<table><tr><td colspan='2'>[[4lu6]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LU6 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>

<tr><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=1.14.14.7 1.14.14.7] </span></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lu6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lu6 PDBsum]</span></td></tr>

<table>

== 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.

~~The entry 4lu6 is ON HOLD until Paper Publication~~

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>

~~Authors: Poor~~, C.B., Lewis, J.C.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: ~~Thermostabilized RebH~~

== References ==

__TOC__

</StructureSection>

[[Category: Tryptophan 7-halogenase]]

[[Category: Lewis, J C.]]

[[Category: Poor, C B.]]

[[Category: Halogenase]]

[[Category: Oxidoreductase]]

[[Category: Themrostability]]

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-'''Unreleased structure'''
+==Thermostabilized RebH==
+<StructureSection load='4lu6' size='340' side='right' caption='[[4lu6]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4lu6]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LU6 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
+<tr><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=1.14.14.7 1.14.14.7] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lu6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lu6 PDBsum]</span></td></tr>
+<table>
+<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.
-The entry 4lu6 is ON HOLD  until Paper Publication
+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>
-Authors: Poor, C.B., Lewis, J.C.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Thermostabilized RebH
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Tryptophan 7-halogenase]]
+[[Category: Lewis, J C.]]
+[[Category: Poor, C B.]]
+[[Category: Halogenase]]
+[[Category: Oxidoreductase]]
+[[Category: Themrostability]]