8q5f
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8q5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q5f OCA], [https://pdbe.org/8q5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q5f RCSB], [https://www.ebi.ac.uk/pdbsum/8q5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q5f 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=8q5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q5f OCA], [https://pdbe.org/8q5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q5f RCSB], [https://www.ebi.ac.uk/pdbsum/8q5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q5f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Most flavin-dependent enzymes contain a dissociable flavin cofactor. We present a new approach for installing in vivo a covalent bond between a flavin cofactor and its host protein. By using a flavin transferase and carving a flavinylation motif in target proteins, we demonstrate that "dissociable" flavoproteins can be turned into covalent flavoproteins. Specifically, four different flavin mononucleotide-containing proteins were engineered to undergo covalent flavinylation: a light-oxygen-voltage domain protein, a mini singlet oxygen generator, a nitroreductase, and an old yellow enzyme-type ene reductase. Optimizing the flavinylation motif and expression conditions led to the covalent flavinylation of all four flavoproteins. The engineered covalent flavoproteins retained function and often exhibited improved performance, such as higher thermostability or catalytic performance. The crystal structures of the designed covalent flavoproteins confirmed the designed threonyl-phosphate linkage. The targeted flavoproteins differ in fold and function, indicating that this method of introducing a covalent flavin-protein bond is a powerful new method to create flavoproteins that cannot lose their cofactor, boosting their performance. | ||
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| + | Fixing Flavins: Hijacking a Flavin Transferase for Equipping Flavoproteins with a Covalent Flavin Cofactor.,Tong Y, Kaya SG, Russo S, Rozeboom HJ, Wijma HJ, Fraaije MW J Am Chem Soc. 2023 Dec 13;145(49):27140-27148. doi: 10.1021/jacs.3c12009. Epub , 2023 Dec 4. PMID:38048072<ref>PMID:38048072</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8q5f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of miniSOG protein from Arabidopsis thaliana with covalent FMN
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