8xhq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The complex structure of SoBcmC and its natural substrate== |
| + | <StructureSection load='8xhq' size='340' side='right'caption='[[8xhq]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8xhq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_ossamyceticus Streptomyces ossamyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XHQ 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]] 1.9000065Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LVE:(3~{S},6~{S})-3-(2-methylpropyl)-6-[(2~{S})-4-oxidanylbutan-2-yl]piperazine-2,5-dione'>A1LVE</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=8xhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xhq OCA], [https://pdbe.org/8xhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xhq RCSB], [https://www.ebi.ac.uk/pdbsum/8xhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xhq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The C-H bond functionalization has been widely used in chemical synthesis over the past decade. However, regio- and stereoselectivity still remain a significant challenge, especially for inert aliphatic C-H bonds. Here we report the mechanism of three Fe(II)/alpha-ketoglutarate-dependent dioxygenases in bicyclomycin synthesis, which depicts the natural tactic to sequentially hydroxylate specific C-H bonds of similar substrates (cyclodipeptides). Molecular basis by crystallographic studies, computational simulations, and site-directed mutagenesis reveals the exquisite arrangement of three enzymes using mutually orthogonal strategies to realize three different regio-selectivities. Moreover, this programmable selective hydroxylation can be extended to other cyclodipeptides. This evidence not only provides a naturally occurring showcase corresponding to the widely used methods in chemical catalysis but also expands the toolbox of biocatalysts to address the regioselective functionalization of C-H bonds. | ||
| - | + | Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.,Wu L, He JB, Wei W, Pan HX, Wang X, Yang S, Liang Y, Tang GL, Zhou J Nat Commun. 2025 May 19;16(1):4651. doi: 10.1038/s41467-025-58997-8. PMID:40389404<ref>PMID:40389404</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8xhq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces ossamyceticus]] | ||
| + | [[Category: Tang GL]] | ||
| + | [[Category: Wu L]] | ||
| + | [[Category: Zhou JH]] | ||
Current revision
The complex structure of SoBcmC and its natural substrate
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