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==Structure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently bound== | ==Structure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently bound== | ||
<StructureSection load='5t6m' size='340' side='right' caption='[[5t6m]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5t6m' size='340' side='right'caption='[[5t6m]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5t6m]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T6M FirstGlance]. <br> | <table><tr><td colspan='2'>[[5t6m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T6M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78U:(BETAS)-BETA-METHYL-L-TRYPTOPHAN'>78U</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78U:(BETAS)-BETA-METHYL-L-TRYPTOPHAN'>78U</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dvz|5dvz]], [[5dw3|5dw3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dvz|5dvz]], [[5dw3|5dw3]]</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=2261 ATCC 43587])</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='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=5t6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6m OCA], [http://pdbe.org/5t6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t6m RCSB], [http://www.ebi.ac.uk/pdbsum/5t6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6m 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=5t6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6m OCA], [http://pdbe.org/5t6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t6m RCSB], [http://www.ebi.ac.uk/pdbsum/5t6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6m ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5t6m" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5t6m" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tryptophan synthase|Tryptophan synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43587]] | |||
[[Category: Large Structures]] | |||
[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
[[Category: Arnold, F H]] | [[Category: Arnold, F H]] | ||
Revision as of 15:28, 25 December 2019
Structure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently boundStructure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently bound
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 PubMedTryptophan synthase (TrpS) catalyzes the final steps in the biosynthesis of l-tryptophan from l-serine (Ser) and indole-3-glycerol phosphate (IGP). We report that native TrpS can also catalyze a productive reaction with l-threonine (Thr), leading to (2S,3S)-beta-methyltryptophan. Surprisingly, beta-substitution occurs in vitro with a 3.4-fold higher catalytic efficiency for Ser over Thr using saturating indole, despite a >82000-fold preference for Ser in direct competition using IGP. Structural data identify a novel product binding site, and kinetic experiments clarify the atypical mechanism of specificity: Thr binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle. Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.,Buller AR, van Roye P, Murciano-Calles J, Arnold FH Biochemistry. 2016 Dec 27;55(51):7043-7046. doi: 10.1021/acs.biochem.6b01127., Epub 2016 Dec 13. PMID:27935677[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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