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| | <StructureSection load='5ixj' size='340' side='right'caption='[[5ixj]], [[Resolution|resolution]] 1.54Å' scene=''> | | <StructureSection load='5ixj' size='340' side='right'caption='[[5ixj]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ixj]] 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=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> | + | <table><tr><td colspan='2'>[[5ixj]] 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=5IXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</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='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=THR:THREONINE'>THR</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ixj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ixj OCA], [https://pdbe.org/5ixj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ixj RCSB], [https://www.ebi.ac.uk/pdbsum/5ixj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ixj ProSAT]</span></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> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tryptophan synthase|Tryptophan synthase]] | + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyrfu]] | + | [[Category: Pyrococcus furiosus DSM 3638]] |
| - | [[Category: Tryptophan synthase]]
| + | [[Category: Arnold FH]] |
| - | [[Category: Arnold, F H]] | + | [[Category: Buller AR]] |
| - | [[Category: Buller, A R]] | + | [[Category: Herger M]] |
| - | [[Category: Herger, M]] | + | |
| - | [[Category: Fold-type ii]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Plp]]
| + | |
| - | [[Category: Substrate analog]]
| + | |
| Structural highlights
Function
TRPB1_PYRFU The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Herger M, van Roye P, Romney DK, Brinkmann-Chen S, Buller AR, Arnold FH. Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase. J Am Chem Soc. 2016 Jul 13;138(27):8388-91. doi: 10.1021/jacs.6b04836. Epub 2016 , Jul 1. PMID:27355405 doi:http://dx.doi.org/10.1021/jacs.6b04836
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