8cjh

</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=8cjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cjh OCA], [https://pdbe.org/8cjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cjh RCSB], [https://www.ebi.ac.uk/pdbsum/8cjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cjh ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The genotoxin colibactin produced by Escherichia coli is involved in the development of colorectal cancers. This secondary metabolite is synthesized by a multi-protein machinery, mainly composed of non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) enzymes. In order to decipher the function of a PKS-NRPS hybrid enzyme implicated in a key step of colibactin biosynthesis, we conducted an extensive structural characterization of the ClbK megaenzyme. Here we present the crystal structure of the complete trans-AT PKS module of ClbK showing structural specificities of hybrid enzymes. In addition, we report the SAXS solution structure of the full-length ClbK hybrid that reveals a dimeric organization as well as several catalytic chambers. These results provide a structural framework for the transfer of a colibactin precursor through a PKS-NRPS hybrid enzyme and can pave the way for re-engineering PKS-NRPS hybrid megaenzymes to generate diverse metabolites with many applications.

Architecture of a PKS-NRPS hybrid megaenzyme involved in the biosynthesis of the genotoxin colibactin.,Bonhomme S, Contreras-Martel C, Dessen A, Macheboeuf P Structure. 2023 Apr 4:S0969-2126(23)00095-3. doi: 10.1016/j.str.2023.03.012. PMID:37059096<ref>PMID:37059096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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