6e6u

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'''Unreleased structure'''
 
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The entry 6e6u is ON HOLD until Paper Publication
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==Variant C89S of Dieckmann cyclase, NcmC==
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<StructureSection load='6e6u' size='340' side='right'caption='[[6e6u]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6e6u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharothrix_syringae Saccharothrix syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6u OCA], [https://pdbe.org/6e6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6u RCSB], [https://www.ebi.ac.uk/pdbsum/6e6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A1X9WEN9_SACSY A0A1X9WEN9_SACSY]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Authors: Cogan, D.P., Nair, S.K.
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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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Description: Variant C89S of Dieckmann cyclase, NcmC
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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: Cogan, D.P]]
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<div class="pdbe-citations 6e6u" style="background-color:#fffaf0;"></div>
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[[Category: Nair, S.K]]
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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: Large Structures]]
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[[Category: Saccharothrix syringae]]
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[[Category: Cogan DP]]
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[[Category: Nair SK]]

Current revision

Variant C89S of Dieckmann cyclase, NcmC

PDB ID 6e6u

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