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6e6y
From Proteopedia
(Difference between revisions)
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<StructureSection load='6e6y' size='340' side='right'caption='[[6e6y]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6e6y' size='340' side='right'caption='[[6e6y]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6e6y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51364 Atcc 51364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6Y OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6e6y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51364 Atcc 51364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E6Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6y OCA], [http://pdbe.org/6e6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e6y RCSB], [http://www.ebi.ac.uk/pdbsum/6e6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6y ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | While several bioactive natural products that contain tetramate or pyridone heterocycles have been described, information on the enzymology underpinning these functionalities has been limited. Here we biochemically characterize an off-loading Dieckmann cyclase, NcmC, that installs the tetramate headgroup in nocamycin, a hybrid polyketide/nonribosomal peptide natural product. Crystal structures of the enzyme (1.6 A) and its covalent complex with the epoxide cerulenin (1.6 A) guide additional structure-based mutagenesis and product-profile analyses. Our results offer mechanistic insights into how the conserved thioesterase-like scaffold has been adapted to perform a new chemical reaction, namely, heterocyclization. Additional bioinformatics combined with docking and modeling identifies likely candidates for heterocycle formation in underexplored gene clusters and uncovers a modular basis of substrate recognition by the two subdomains of these Dieckmann cyclases. | ||
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| + | Structural Basis for Enzymatic Off-Loading of Hybrid Polyketides by Dieckmann Condensation.,Cogan DP, Ly J, Nair SK ACS Chem Biol. 2020 Oct 16;15(10):2783-2791. doi: 10.1021/acschembio.0c00579., Epub 2020 Oct 5. PMID:33017142<ref>PMID:33017142</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6e6y" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:29, 21 October 2020
Dieckmann cyclase, NcmC
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