View source for 3tsy

==4-Coumaroyl-CoA Ligase::Stilbene Synthase fusion protein==
<StructureSection load='3tsy' size='340' side='right' caption='[[3tsy]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tsy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TSY FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a9u|3a9u]], [[3a9v|3a9v]], [[1xes|1xes]], [[1z1e|1z1e]]</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">4CL1, At1g51680, At4CL1, F19C24.11, VvSTS, STS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tsy RCSB], [http://www.ebi.ac.uk/pdbsum/3tsy PDBsum]</span></td></tr>
<table>
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== Publication Abstract from PubMed ==
To increase the biochemical efficiency of biosynthetic systems, metabolic engineers have explored different approaches for organizing enzymes, including the generation of unnatural fusion proteins. Previous work aimed at improving the biosynthesis of resveratrol, a stilbene associated a range of health-promoting activities, in yeast used an unnatural engineered fusion protein of Arabidopsis thaliana (thale cress) 4-coumaroyl-CoA ligase (At4CL1) and Vitis vinifera (grape) stilbene synthase (VvSTS) to increase resveratrol levels 15-fold relative to yeast expressing the individual enzymes. Here we present the crystallographic and biochemical analysis of the 4CL::STS fusion protein. Determination of the X-ray crystal structure of 4CL::STS provides the first molecular view of an artificial didomain adenylation/ketosynthase fusion protein. Comparison of the steady-state kinetic properties of At4CL1, VvSTS, and 4CL::STS demonstrates that the fusion protein improves catalytic efficiency of either reaction less than 3-fold. Structural and kinetic analysis suggests that colocalization of the two enzyme active sites within 70 A of each other provides the basis for enhanced in vivo synthesis of resveratrol.

Structural and Kinetic Analysis of the Unnatural Fusion Protein 4-Coumaroyl-CoA Ligase::Stilbene Synthase.,Wang Y, Yi H, Wang M, Yu O, Jez JM J Am Chem Soc. 2011 Dec 5. PMID:22129213<ref>PMID:22129213</ref>

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Arath]]
[[Category: Jez, J M.]]
[[Category: Yi, H.]]
[[Category: Fusion protein]]
[[Category: Ligase]]
[[Category: Transferase]]