5dw3: Difference between revisions
New page: '''Unreleased structure''' The entry 5dw3 is ON HOLD Authors: Buller, A.R., Arnold, F.H. Description: Tryptophan Synthase beta-subunit from Pyrococcus furiosus with product L-tryptopha... |
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The | ==Tryptophan Synthase beta-subunit from Pyrococcus furiosus with product L-tryptophan non-covalently bound in the active site== | ||
<StructureSection load='5dw3' size='340' side='right'caption='[[5dw3]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dw3]] 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=5DW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DW3 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]] 1.74Å</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>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=5dw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw3 OCA], [https://pdbe.org/5dw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dw3 RCSB], [https://www.ebi.ac.uk/pdbsum/5dw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dw3 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 == | |||
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<ref>PMID:26553994</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5dw3" style="background-color:#fffaf0;"></div> | ||
[[Category: Arnold | |||
==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: Buller AR]] | |||
Latest revision as of 01:02, 29 June 2023
Tryptophan Synthase beta-subunit from Pyrococcus furiosus with product L-tryptophan non-covalently bound in the active siteTryptophan Synthase beta-subunit from Pyrococcus furiosus with product L-tryptophan non-covalently bound in the active site
Structural highlights
FunctionTRPB1_PYRFU The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). Publication Abstract from PubMedEnzymes 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 AlsoReferences
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