View source for 8xhy


==The complex structure of mutant T307A of SsBcmE and its natural substrate cIL==
<StructureSection load='8xhy' size='340' side='right'caption='[[8xhy]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xhy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cinnamoneus Streptomyces cinnamoneus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XHY 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]] 1.7100197&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LVH:(3~{S},6~{S})-3-[(2~{S})-butan-2-yl]-6-(2-methylpropyl)piperazine-2,5-dione'>A1LVH</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8xhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xhy OCA], [https://pdbe.org/8xhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xhy RCSB], [https://www.ebi.ac.uk/pdbsum/8xhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xhy 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xhy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cinnamoneus]]
[[Category: Tang GL]]
[[Category: Wu L]]
[[Category: Zhou JH]]