7jsd
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Hydroxylase homolog of BesD with Fe(II), alpha-ketoglutarate, and lysine== | |
| + | <StructureSection load='7jsd' size='340' side='right'caption='[[7jsd]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7jsd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_roseifaciens Streptomyces roseifaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JSD 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]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=7jsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jsd OCA], [https://pdbe.org/7jsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jsd RCSB], [https://www.ebi.ac.uk/pdbsum/7jsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jsd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fe(II)/alpha-ketoglutarate (Fe(II)/alphaKG)-dependent enzymes offer a promising biocatalytic platform for halogenation chemistry owing to their ability to functionalize unactivated C-H bonds. However, relatively few radical halogenases have been identified to date, limiting their synthetic utility. Here, we report a strategy to expand the palette of enzymatic halogenation by engineering a reaction pathway rather than substrate selectivity. This approach could allow us to tap the broader class of Fe(II)/alphaKG-dependent hydroxylases as catalysts by their conversion to halogenases. Toward this goal, we discovered active halogenases from a DNA shuffle library generated from a halogenase-hydroxylase pair using a high-throughput in vivo fluorescent screen coupled to an alkyne-producing biosynthetic pathway. Insights from sequencing halogenation-active variants along with the crystal structure of the hydroxylase enabled engineering of a hydroxylase to perform halogenation with comparable activity and higher selectivity than the wild-type halogenase, showcasing the potential of harnessing hydroxylases for biocatalytic halogenation. | ||
| - | + | Reaction pathway engineering converts a radical hydroxylase into a halogenase.,Neugebauer ME, Kissman EN, Marchand JA, Pelton JG, Sambold NA, Millar DC, Chang MCY Nat Chem Biol. 2022 Feb;18(2):171-179. doi: 10.1038/s41589-021-00944-x. Epub 2021, Dec 22. PMID:34937913<ref>PMID:34937913</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7jsd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces roseifaciens]] | ||
| + | [[Category: Chang MCY]] | ||
| + | [[Category: Kissman EN]] | ||
| + | [[Category: Neugebauer ME]] | ||
Current revision
Hydroxylase homolog of BesD with Fe(II), alpha-ketoglutarate, and lysine
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