5ixj: Difference between revisions
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The | ==Tryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active site== | ||
<StructureSection load='5ixj' size='340' side='right' caption='[[5ixj]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ixj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IXJ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=5ixj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ixj OCA], [http://pdbe.org/5ixj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ixj RCSB], [http://www.ebi.ac.uk/pdbsum/5ixj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ixj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/TRPB1_PYRFU TRPB1_PYRFU]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report that l-threonine may substitute for l-serine in the beta-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-beta-methyltryptophan (beta-MeTrp) in a single step. The trace activity of the wild-type beta-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this increase is correlated with stabilization of the electrophilic aminoacrylate intermediate. The engineered biocatalyst also reacts with a variety of indole analogues and thiophenol for diastereoselective C-C, C-N, and C-S bond-forming reactions. This new activity circumvents the 3-enzyme pathway that produces beta-MeTrp in nature and offers a simple and expandable route to preparing derivatives of this valuable building block. | |||
Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.,Herger M, van Roye P, Romney DK, Brinkmann-Chen S, Buller AR, Arnold FH J Am Chem Soc. 2016 Jul 13;138(27):8388-91. doi: 10.1021/jacs.6b04836. Epub 2016 , Jul 1. PMID:27355405<ref>PMID:27355405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ixj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Tryptophan synthase]] | |||
[[Category: Arnold, F H]] | |||
[[Category: Buller, A R]] | |||
[[Category: Herger, M]] | |||
[[Category: Fold-type ii]] | |||
[[Category: Lyase]] | |||
[[Category: Plp]] | |||
[[Category: Substrate analog]] | |||
Revision as of 00:04, 10 September 2016
Tryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active site
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