5ugz

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'''Unreleased structure'''
 
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The entry 5ugz is ON HOLD until Paper Publication
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==Crystal structure of ClbQ from the colibactin NRPS/PKS pathway==
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<StructureSection load='5ugz' size='340' side='right' caption='[[5ugz]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ugz]] is a 2 chain structure. 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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Guntaka, N.S., Bruner, S.D.
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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<ref>PMID:28846367</ref>
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Description: Crystal structure of ClbQ from the colibactin NRPS/PKS pathway
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Bruner, S.D]]
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<div class="pdbe-citations 5ugz" style="background-color:#fffaf0;"></div>
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[[Category: Guntaka, N.S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bruner, S D]]
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[[Category: Guntaka, N S]]
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[[Category: Colibactin]]
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[[Category: Hydrolase]]
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[[Category: Type-ii thioesterase]]

Revision as of 04:33, 21 September 2017

Crystal structure of ClbQ from the colibactin NRPS/PKS pathway

5ugz, resolution 1.98Å

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