5b6i
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of fluorinase from Streptomyces sp. MA37== | |
| + | <StructureSection load='5b6i' size='340' side='right' caption='[[5b6i]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b6i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B6I FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></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=5b6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6i OCA], [http://pdbe.org/5b6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b6i RCSB], [http://www.ebi.ac.uk/pdbsum/5b6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fluorinases offer an environmentally friendly alternative for selective fluorination under mild conditions. However, their diversity is limited in nature and they have yet to be engineered through directed evolution. Herein, we report the directed evolution of the fluorinase FlA1 for improved conversion of the non-native substrate 5'-chloro-5'-deoxyadenosine (5'-ClDA) into 5'-fluoro-5'-deoxyadenosine (5'-FDA). The evolved variants, fah2081 (A279Y) and fah2114 (F213Y, A279L), were successfully applied in the radiosynthesis of 5'-[18 F]FDA, with overall radiochemical conversion (RCC) more than 3-fold higher than wild-type FlA1. Kinetic studies of the two-step reaction revealed that the variants show a significantly improved kcat value in the conversion of 5'-ClDA into S-adenosyl-l-methionine (SAM) but a reduced kcat value in the conversion of SAM into 5'-FDA. | ||
| - | + | Directed Evolution of a Fluorinase for Improved Fluorination Efficiency with a Non-native Substrate.,Sun H, Yeo WL, Lim YH, Chew X, Smith DJ, Xue B, Chan KP, Robinson RC, Robins EG, Zhao H, Ang EL Angew Chem Int Ed Engl. 2016 Oct 14. doi: 10.1002/anie.201606722. PMID:27739177<ref>PMID:27739177</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Robinson, R | + | <div class="pdbe-citations 5b6i" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Robinson, R C]] | ||
[[Category: Xue, B]] | [[Category: Xue, B]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 18:27, 26 October 2016
Structure of fluorinase from Streptomyces sp. MA37
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