5t6m: Difference between revisions

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'''Unreleased structure'''


The entry 5t6m is ON HOLD
==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]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5t6m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5T6M 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=78U:(BETAS)-BETA-METHYL-L-TRYPTOPHAN'>78U</scene>, <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></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=5t6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6m OCA], [https://pdbe.org/5t6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t6m RCSB], [https://www.ebi.ac.uk/pdbsum/5t6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6m 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 ==
Tryptophan 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 &gt;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.


Authors:  
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<ref>PMID:27935677</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5t6m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Arnold FH]]
[[Category: Buller AR]]
[[Category: Van Roye P]]
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