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'''Unreleased structure'''


The entry 8xhp is ON HOLD
==The apo structure of SsBcmC==
<StructureSection load='8xhp' size='340' side='right'caption='[[8xhp]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xhp]] is a 3 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=8XHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XHP 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]] 1.8600082&#8491;</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=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=8xhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xhp OCA], [https://pdbe.org/8xhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xhp RCSB], [https://www.ebi.ac.uk/pdbsum/8xhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xhp 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.


Authors: Wu, L., Tang, G.L., Zhou, J.H.
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>


Description: The apo structure of SsBcmC
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Tang, G.L]]
<div class="pdbe-citations 8xhp" style="background-color:#fffaf0;"></div>
[[Category: Wu, L]]
== References ==
[[Category: Zhou, J.H]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cinnamoneus]]
[[Category: Tang GL]]
[[Category: Wu L]]
[[Category: Zhou JH]]
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