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8ejy

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'''Unreleased structure'''
 
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The entry 8ejy is ON HOLD until Paper Publication
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==[4+2] Aza-Cyclase F293A variant==
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<StructureSection load='8ejy' size='340' side='right'caption='[[8ejy]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ejy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planobispora_rosea Planobispora rosea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EJY FirstGlance]. <br>
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</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=8ejy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ejy OCA], [https://pdbe.org/8ejy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ejy RCSB], [https://www.ebi.ac.uk/pdbsum/8ejy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ejy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/U5Q3T2_PLARO U5Q3T2_PLARO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Thiazole-containing pyritides (thiopeptides) are ribosomally synthesized and post-translationally modified peptides (RiPPs) that have attracted interest owing to their potent biological activities and structural complexity. The class-defining feature of a thiopeptide is a six-membered, nitrogenous heterocycle formed by an enzymatic [4 + 2]-cycloaddition. In rare cases, piperidine or dehydropiperidine (DHP) is present; however, the aromatized pyridine is considerably more common. Despite significant effort, the mechanism by which the central pyridine is formed remains poorly understood. Building on our recent observation of the Bycroft-Gowland intermediate (i.e., the direct product of the [4 + 2]-cycloaddition), we interrogated thiopeptide pyridine synthases using a combination of targeted mutagenesis, kinetic assays, substrate analogs, enzyme-substrate cross-linking, and chemical rescue experiments. Collectively, our data delineate roles for several conserved residues in thiopeptide pyridine synthases. A critical tyrosine facilitates the final aromatization step of pyridine formation. This work provides a foundation for further exploration of the [4 + 2]-cycloaddition reaction and future customization of pyridine-containing macrocyclic peptides.
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Authors: Nair, S.K.
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Enzymatic Pyridine Aromatization during Thiopeptide Biosynthesis.,Rice AJ, Pelton JM, Kramer NJ, Catlin DS, Nair SK, Pogorelov TV, Mitchell DA, Bowers AA J Am Chem Soc. 2022 Nov 23;144(46):21116-21124. doi: 10.1021/jacs.2c07377. Epub , 2022 Nov 9. PMID:36351243<ref>PMID:36351243</ref>
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Description: [4+2] Aza-Cyclase F293A variant
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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: Nair, S.K]]
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<div class="pdbe-citations 8ejy" style="background-color:#fffaf0;"></div>
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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: Planobispora rosea]]
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[[Category: Nair SK]]

Revision as of 10:15, 24 November 2022

[4+2] Aza-Cyclase F293A variant

PDB ID 8ejy

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