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| | ==X-ray crystal structure of tryptophan synthase complex from Pyrococcus furiosus at 2.76 A== | | ==X-ray crystal structure of tryptophan synthase complex from Pyrococcus furiosus at 2.76 A== |
| - | <StructureSection load='5e0k' size='340' side='right' caption='[[5e0k]], [[Resolution|resolution]] 2.76Å' scene=''> | + | <StructureSection load='5e0k' size='340' side='right'caption='[[5e0k]], [[Resolution|resolution]] 2.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e0k]] is a 12 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=5E0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E0K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e0k]] is a 12 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=5E0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E0K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.76Å</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dvz|5dvz]], [[5dw0|5dw0]], [[5dw3|5dw3]]</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=5e0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e0k OCA], [https://pdbe.org/5e0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e0k RCSB], [https://www.ebi.ac.uk/pdbsum/5e0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e0k ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpA, PF1705 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), trpB1, PF1706 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=5e0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e0k OCA], [http://pdbe.org/5e0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e0k RCSB], [http://www.ebi.ac.uk/pdbsum/5e0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e0k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRPA_PYRFU TRPA_PYRFU]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[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/TRPA_PYRFU TRPA_PYRFU] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5e0k" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5e0k" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| | == References == | | == References == |
| | <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: Buller, A R]] | + | [[Category: Buller AR]] |
| - | [[Category: Murciano-Calles, J]] | + | [[Category: Murciano-Calles J]] |
| - | [[Category: Complex]]
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| - | [[Category: Enzyme]]
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| - | [[Category: Lyase]]
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| - | [[Category: Plp]]
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| Structural highlights
Function
TRPA_PYRFU The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Publication Abstract from PubMed
Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the beta-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native alphabetabetaalpha complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the alpha-subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the alpha-subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope.
Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation.,Buller AR, Brinkmann-Chen S, Romney DK, Herger M, Murciano-Calles J, Arnold FH Proc Natl Acad Sci U S A. 2015 Nov 24;112(47):14599-604. doi:, 10.1073/pnas.1516401112. Epub 2015 Nov 9. PMID:26553994[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Buller AR, Brinkmann-Chen S, Romney DK, Herger M, Murciano-Calles J, Arnold FH. Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation. Proc Natl Acad Sci U S A. 2015 Nov 24;112(47):14599-604. doi:, 10.1073/pnas.1516401112. Epub 2015 Nov 9. PMID:26553994 doi:http://dx.doi.org/10.1073/pnas.1516401112
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