5dw0

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==TrpB from Pyrococcus furiosus with L-serine bound as the external aldimine==
==TrpB from Pyrococcus furiosus with L-serine bound as the external aldimine==
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<StructureSection load='5dw0' size='340' side='right' caption='[[5dw0]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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<StructureSection load='5dw0' size='340' side='right'caption='[[5dw0]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dw0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DW0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dw0]] 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=5DW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DW0 FirstGlance]. <br>
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</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=PLS:[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE'>PLS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dvz|5dvz]], [[5dw3|5dw3]], [[5e0k|5e0k]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLS:[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE'>PLS</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw0 OCA], [https://pdbe.org/5dw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dw0 RCSB], [https://www.ebi.ac.uk/pdbsum/5dw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dw0 ProSAT]</span></td></tr>
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<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=5dw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw0 OCA], [http://pdbe.org/5dw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dw0 RCSB], [http://www.ebi.ac.uk/pdbsum/5dw0 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
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<div class="pdbe-citations 5dw0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Tryptophan synthase]]
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[[Category: Large Structures]]
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[[Category: Arnold, F H]]
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[[Category: Pyrococcus furiosus DSM 3638]]
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[[Category: Buller, A R]]
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[[Category: Arnold FH]]
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[[Category: External aldimine]]
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[[Category: Buller AR]]
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[[Category: Lyase]]
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[[Category: Plp]]
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[[Category: Pr]]
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Current revision

TrpB from Pyrococcus furiosus with L-serine bound as the external aldimine

PDB ID 5dw0

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