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==Engineered Holo TrpB from Pyrococcus furiosus, PfTrpB7E6 with (2S,3S)-isopropylserine bound as the external aldimine==
==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]] 1.77&Aring;' scene=''>
<StructureSection load='6cut' size='340' side='right'caption='[[6cut]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6cut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. 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>
<table><tr><td colspan='2'>[[6cut]] 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=6CUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpB1, PF1706 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cut OCA], [https://pdbe.org/6cut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cut RCSB], [https://www.ebi.ac.uk/pdbsum/6cut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cut ProSAT]</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>
</table>
== Function ==
== 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).  
[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 6cut" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tryptophan synthase|Tryptophan synthase]]
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrfu]]
[[Category: Large Structures]]
[[Category: Tryptophan synthase]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Arnold, F H]]
[[Category: Arnold FH]]
[[Category: Boville, C E]]
[[Category: Boville CE]]
[[Category: Buller, A R]]
[[Category: Buller AR]]
[[Category: Scheele, R A]]
[[Category: Scheele RA]]
[[Category: External aldimine]]
[[Category: Lyase]]

Latest revision as of 17:30, 13 March 2024

Engineered Holo TrpB from Pyrococcus furiosus, PfTrpB7E6 with (2S,3S)-isopropylserine bound as the external aldimineEngineered Holo TrpB from Pyrococcus furiosus, PfTrpB7E6 with (2S,3S)-isopropylserine bound as the external aldimine

Structural highlights

6cut is a 4 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.77Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPB1_PYRFU The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity).

See Also

6cut, resolution 1.77Å

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