8jz4: Difference between revisions
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==Crystal structure of AetF in complex with FAD and 5-bromo-L-tryptophan== | |||
<StructureSection load='8jz4' size='340' side='right'caption='[[8jz4]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8jz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aetokthonos_hydrillicola_Thurmond2011 Aetokthonos hydrillicola Thurmond2011]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JZ4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=64X:5-bromo-L-tryptophan'>64X</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=8jz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jz4 OCA], [https://pdbe.org/8jz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jz4 RCSB], [https://www.ebi.ac.uk/pdbsum/8jz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jz4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A861B9Z9_9CYAN A0A861B9Z9_9CYAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Flavin-dependent halogenases (FDHs) have tremendous applications in synthetic chemistry. A single-component FDH, AetF, exhibits both halogenase and reductase activities in a continuous polypeptide chain. AetF exhibits broad substrate promiscuity and catalyzes the two-step bromination of l-tryptophan (l-Trp) to produce 5-bromotryptophan (5-Br-Trp) and 5,7-dibromo-l-tryptophan (5,7-di-Br-Trp). To elucidate the mechanism of action of AetF, we solved its crystal structure in complex with FAD, FAD/NADP(+), FAD/l-Trp, and FAD/5-Br-Trp at resolutions of 1.92-2.23 A. The obtained crystal structures depict the unprecedented topology of single-component FDH. Structural analysis revealed that the substrate flexibility and dibromination capability of AetF could be attributed to its spacious substrate-binding pocket. In addition, highly-regulated interaction networks between the substrate-recognizing residues and 5-Br-Trp are crucial for the dibromination activity of AetF. Several Ala variants underwent monobromination with >98 % C5-regioselectivity toward l-Trp. These results reveal the catalytic mechanism of single-component FDH for the first time and contribute to efficient FDH protein engineering for biocatalytic halogenation. | |||
Structural and functional insights into the self-sufficient flavin-dependent halogenase.,Dai L, Li H, Dai S, Zhang Q, Zheng H, Hu Y, Guo RT, Chen CC Int J Biol Macromol. 2024 Mar;260(Pt 1):129312. doi: , 10.1016/j.ijbiomac.2024.129312. Epub 2024 Jan 10. PMID:38216020<ref>PMID:38216020</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8jz4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aetokthonos hydrillicola Thurmond2011]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen C-C]] | |||
[[Category: Dai L]] | |||
[[Category: Guo R-T]] | |||
[[Category: Li H]] | |||
Latest revision as of 08:57, 5 June 2024
Crystal structure of AetF in complex with FAD and 5-bromo-L-tryptophanCrystal structure of AetF in complex with FAD and 5-bromo-L-tryptophan
Structural highlights
FunctionPublication Abstract from PubMedFlavin-dependent halogenases (FDHs) have tremendous applications in synthetic chemistry. A single-component FDH, AetF, exhibits both halogenase and reductase activities in a continuous polypeptide chain. AetF exhibits broad substrate promiscuity and catalyzes the two-step bromination of l-tryptophan (l-Trp) to produce 5-bromotryptophan (5-Br-Trp) and 5,7-dibromo-l-tryptophan (5,7-di-Br-Trp). To elucidate the mechanism of action of AetF, we solved its crystal structure in complex with FAD, FAD/NADP(+), FAD/l-Trp, and FAD/5-Br-Trp at resolutions of 1.92-2.23 A. The obtained crystal structures depict the unprecedented topology of single-component FDH. Structural analysis revealed that the substrate flexibility and dibromination capability of AetF could be attributed to its spacious substrate-binding pocket. In addition, highly-regulated interaction networks between the substrate-recognizing residues and 5-Br-Trp are crucial for the dibromination activity of AetF. Several Ala variants underwent monobromination with >98 % C5-regioselectivity toward l-Trp. These results reveal the catalytic mechanism of single-component FDH for the first time and contribute to efficient FDH protein engineering for biocatalytic halogenation. Structural and functional insights into the self-sufficient flavin-dependent halogenase.,Dai L, Li H, Dai S, Zhang Q, Zheng H, Hu Y, Guo RT, Chen CC Int J Biol Macromol. 2024 Mar;260(Pt 1):129312. doi: , 10.1016/j.ijbiomac.2024.129312. Epub 2024 Jan 10. PMID:38216020[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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