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| | <StructureSection load='5b6i' size='340' side='right'caption='[[5b6i]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='5b6i' size='340' side='right'caption='[[5b6i]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b6i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp._ma37 Streptomyces sp. ma37]. 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> | + | <table><tr><td colspan='2'>[[5b6i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._MA37 Streptomyces sp. MA37]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1400207 Streptomyces sp. MA37])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6i OCA], [https://pdbe.org/5b6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b6i RCSB], [https://www.ebi.ac.uk/pdbsum/5b6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/W0W999_9ACTN W0W999_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces sp. ma37]] | + | [[Category: Streptomyces sp. MA37]] |
| - | [[Category: Robinson, R C]] | + | [[Category: Robinson RC]] |
| - | [[Category: Xue, B]] | + | [[Category: Xue B]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
W0W999_9ACTN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun H, Yeo WL, Lim YH, Chew X, Smith DJ, Xue B, Chan KP, Robinson RC, Robins EG, Zhao H, Ang EL. Directed Evolution of a Fluorinase for Improved Fluorination Efficiency with a Non-native Substrate. Angew Chem Int Ed Engl. 2016 Oct 14. doi: 10.1002/anie.201606722. PMID:27739177 doi:http://dx.doi.org/10.1002/anie.201606722
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