8ejz: Difference between revisions

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'''Unreleased structure'''


The entry 8ejz is ON HOLD
==[4+2] Aza-Cyclase Y293F variant==
<StructureSection load='8ejz' size='340' side='right'caption='[[8ejz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ejz]] is a 2 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=8EJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EJZ FirstGlance]. <br>
</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=8ejz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ejz OCA], [https://pdbe.org/8ejz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ejz RCSB], [https://www.ebi.ac.uk/pdbsum/8ejz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ejz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U5Q3T2_PLARO U5Q3T2_PLARO]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Nair, S.K.
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>


Description: [4+2] Aza-Cyclase Y293F variant
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Nair, S.K]]
<div class="pdbe-citations 8ejz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Planobispora rosea]]
[[Category: Nair SK]]

Revision as of 10:15, 24 November 2022

[4+2] Aza-Cyclase Y293F variant

8ejz, resolution 1.70Å

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