6cut: Difference between revisions
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The | ==Engineered Holo TrpB from Pyrococcus furiosus, PfTrpB7E6 with (2S,3S)-isopropylserine bound as the external aldimine== | ||
<StructureSection load='6cut' size='340' side='right' caption='[[6cut]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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 == | |||
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. | |||
Engineered biosynthesis of beta-alkyl tryptophan analogs.,Boville CE, Scheele RA, Koch P, Brinkmann-Chen S, Buller AR, Arnold FH Angew Chem Int Ed Engl. 2018 Sep 14. doi: 10.1002/anie.201807998. PMID:30215880<ref>PMID:30215880</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6cut" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Tryptophan synthase]] | |||
[[Category: Arnold, F H]] | |||
[[Category: Boville, C E]] | |||
[[Category: Buller, A R]] | |||
[[Category: Scheele, R A]] | |||
[[Category: External aldimine]] | |||
[[Category: Lyase]] | |||
