View source for 6cuv


==Engineered Holo TrpB from Pyrococcus furiosus, PfTrpB7E6==
<StructureSection load='6cuv' size='340' side='right'caption='[[6cuv]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cuv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CUV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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=6cuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cuv OCA], [https://pdbe.org/6cuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cuv RCSB], [https://www.ebi.ac.uk/pdbsum/6cuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cuv ProSAT]</span></td></tr>
</table>
== Function ==
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cuv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Arnold FH]]
[[Category: Boville CE]]
[[Category: Buller AR]]
[[Category: Scheele RA]]