View source for 7lcw


==Aspartimidylated Lasso Peptide Lihuanodin==
<StructureSection load='7lcw' size='340' side='right'caption='[[7lcw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lcw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lihuaxuella_thermophila Lihuaxuella thermophila]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LCW 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=7lcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lcw OCA], [https://pdbe.org/7lcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lcw RCSB], [https://www.ebi.ac.uk/pdbsum/7lcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lcw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1H8GYX0_9BACL A0A1H8GYX0_9BACL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) defined by their threaded structure. Besides the class-defining isopeptide bond, other post-translational modifications (PTMs) that further tailor lasso peptides have been previously reported. Using genome mining tools, we identified a subset of lasso peptide biosynthetic gene clusters (BGCs) that are colocalized with genes encoding protein l-isoaspartyl methyltransferase (PIMT) homologues. PIMTs have an important role in protein repair, restoring isoaspartate residues formed from asparagine deamidation to aspartate. Here we report a new function for PIMT enzymes in the post-translational modification of lasso peptides. The PIMTs associated with lasso peptide BGCs first methylate an l-aspartate side chain found within the ring of the lasso peptide. The methyl ester is then converted into a stable aspartimide moiety, endowing the lasso peptide ring with rigidity relative to its unmodified counterpart. We describe the heterologous expression and structural characterization of two examples of aspartimide-modified lasso peptides from thermophilic Gram-positive bacteria. The lasso peptide cellulonodin-2 is encoded in the genome of actinobacterium Thermobifida cellulosilytica, while lihuanodin is encoded in the genome of firmicute Lihuaxuella thermophila. Additional genome mining revealed PIMT-containing lasso peptide BGCs in 48 organisms. In addition to heterologous expression, we have reconstituted PIMT-mediated aspartimide formation in vitro, showing that lasso peptide-associated PIMTs transfer methyl groups very rapidly as compared to canonical PIMTs. Furthermore, in stark contrast to other characterized lasso peptide PTMs, the methyltransferase functions only on lassoed substrates.

Cellulonodin-2 and Lihuanodin: Lasso Peptides with an Aspartimide Post-Translational Modification.,Cao L, Beiser M, Koos JD, Orlova M, Elashal HE, Schroder HV, Link AJ J Am Chem Soc. 2021 Jul 20. doi: 10.1021/jacs.1c05017. PMID:34283601<ref>PMID:34283601</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lcw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Lihuaxuella thermophila]]
[[Category: Cao L]]
[[Category: Link AJ]]