6cut

<StructureSection load='6cut' size='340' side='right' caption='[[6cut]], [[Resolution|resolution]] 1.77&Aring;' scene=''>

<table><tr><td colspan='2'>[[6cut]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CUT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEJ:(2S,3S)-3-hydroxy-2-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-methylpentanoic+acid+(non-preferred+name)'>FEJ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cut OCA], [http://pdbe.org/6cut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cut RCSB], [http://www.ebi.ac.uk/pdbsum/6cut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cut ProSAT]</span></td></tr>

[[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).

Non-canonical amino acids (ncAAs) with dual stereocenters at the alpha and beta positions are valuable precursors to natural products and therapeutics. Despite the potential applications of such bioactive beta-branched ncAAs, their availability is limited due to the inefficiency of the multi-step methods used to prepare them. Here we report a stereoselective biocatalytic synthesis of beta-branched tryptophan analogs using an engineered variant of Pyrococcus furiosus tryptophan synthase (PfTrpB), PfTrpB7E6. PfTrpB7E6 is the first biocatalyst to synthesize bulky beta-branched tryptophan analogs in a single step, with demonstrated access to 27 ncAAs. The molecular basis for the efficient catalysis and broad substrate tolerance of PfTrpB7E6 was explored through X-ray crystallography and UV-visible light spectroscopy, which revealed that a combination of active-site and remote mutations increase the abundance and persistence of a key reactive intermediate. PfTrpB7E6 provides an operationally simple and environmentally benign platform for preparation of beta-branched tryptophan building blocks.

 

== References ==

[[Category: Tryptophan synthase]]

[[Category: Arnold, F H]]

[[Category: Boville, C E]]

[[Category: Buller, A R]]

[[Category: Scheele, R A]]

[[Category: External aldimine]]

[[Category: Lyase]]