5dw0: Difference between revisions
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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== | ||
<StructureSection load='5dw0' size='340' side='right' caption='[[5dw0]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='5dw0' size='340' side='right'caption='[[5dw0]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dw0]] is a 4 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=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> | <table><tr><td colspan='2'>[[5dw0]] is a 4 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=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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</div> | </div> | ||
<div class="pdbe-citations 5dw0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5dw0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tryptophan synthase|Tryptophan synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pyrfu]] | [[Category: Pyrfu]] | ||
[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
Revision as of 14:28, 25 December 2019
TrpB from Pyrococcus furiosus with L-serine bound as the external aldimineTrpB from Pyrococcus furiosus with L-serine bound as the external aldimine
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 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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