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| | ==Crystal structure of ClbQ from the colibactin NRPS/PKS pathway== | | ==Crystal structure of ClbQ from the colibactin NRPS/PKS pathway== |
| - | <StructureSection load='5ugz' size='340' side='right' caption='[[5ugz]], [[Resolution|resolution]] 1.98Å' scene=''> | + | <StructureSection load='5ugz' size='340' side='right'caption='[[5ugz]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ugz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UGZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ugz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UGZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.983Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clbQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ugz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ugz OCA], [http://pdbe.org/5ugz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ugz RCSB], [http://www.ebi.ac.uk/pdbsum/5ugz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ugz ProSAT]</span></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=5ugz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ugz OCA], [https://pdbe.org/5ugz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ugz RCSB], [https://www.ebi.ac.uk/pdbsum/5ugz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ugz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0P7K7_ECOLX Q0P7K7_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Bruner, S D]] | + | [[Category: Large Structures]] |
| - | [[Category: Guntaka, N S]] | + | [[Category: Bruner SD]] |
| - | [[Category: Colibactin]] | + | [[Category: Guntaka NS]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Type-ii thioesterase]]
| + | |
| Structural highlights
Function
Q0P7K7_ECOLX
Publication Abstract from PubMed
Colibactin is a genotoxic hybrid nonribosomal peptide/polyketide secondary metabolite produced by various pathogenic and probiotic bacteria residing in the human gut. The presence of colibactin metabolites has been correlated to colorectal cancer formation in several studies. The specific function of many gene products in the colibactin gene cluster can be predicted. However, the role of ClbQ, a type II editing thioesterase, has not been established. The importance of ClbQ has been demonstrated by genetic deletions that abolish colibactin cytotoxic activity, and recent studies suggest an atypical role in releasing pathway intermediates from the assembly line. Here we report the 2.0 A crystal structure and biochemical characterization of ClbQ. Our data reveal that ClbQ exhibits greater catalytic efficiency toward acyl-thioester substrates as compared to precolibactin intermediates and does not discriminate among carrier proteins. Cyclized pyridone-containing colibactins, which are off-pathway derivatives, are not viable substrates for ClbQ, while linear precursors are, supporting a role of ClbQ in facilitating the promiscuous off-loading of premature precolibactin metabolites and novel insights into colibactin biosynthesis.
Structure and Functional Analysis of ClbQ, an Unusual Intermediate-Releasing Thioesterase from the Colibactin Biosynthetic Pathway.,Guntaka NS, Healy AR, Crawford JM, Herzon SB, Bruner SD ACS Chem Biol. 2017 Sep 8. doi: 10.1021/acschembio.7b00479. PMID:28846367[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guntaka NS, Healy AR, Crawford JM, Herzon SB, Bruner SD. Structure and Functional Analysis of ClbQ, an Unusual Intermediate-Releasing Thioesterase from the Colibactin Biosynthetic Pathway. ACS Chem Biol. 2017 Sep 8. doi: 10.1021/acschembio.7b00479. PMID:28846367 doi:http://dx.doi.org/10.1021/acschembio.7b00479
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