View source for 8vyc


==Graspetide pre-fuscimiditide A1C/T3C variant==
<StructureSection load='8vyc' size='340' side='right'caption='[[8vyc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vyc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VYC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8vyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vyc OCA], [https://pdbe.org/8vyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vyc RCSB], [https://www.ebi.ac.uk/pdbsum/8vyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vyc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47NX9_THEFY Q47NX9_THEFY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ribosomally synthesized and post-translationally modified peptide (RiPP) superfamily of natural products includes many examples of cyclic peptides with diverse macrocyclization chemistries. The graspetides, one family of macrocyclized RiPPs, harbor side chain-side chain ester or amide linkages. We recently reported the structure and biosynthesis of the graspetide pre-fuscimiditide, a 22-amino-acid (aa) peptide with two ester cross-links forming a stem-loop structure. These cross-links are introduced by a single graspetide synthetase, the ATP-grasp enzyme ThfB. Here we show that ThfB can also catalyze the formation of amide or thioester cross-links in prefuscimiditide, with thioester formation being especially efficient. We further show that upon proteolysis to reveal an N-terminal cysteine residue, the thioester-linked peptide rapidly and quantitatively rearranges via native chemical ligation into an isopeptide-bonded head-to-tail cyclic peptide. The solution structure of this rearranged peptide was determined by using 2D NMR spectroscopy experiments. Our methodology offers a straightforward recombinant route to head-to-tail cyclic peptides.

Cyclic Peptides from Graspetide Biosynthesis and Native Chemical Ligation.,Choi B, Acuna A, Link AJ J Am Chem Soc. 2024 May 1;146(17):11605-11609. doi: 10.1021/jacs.4c02745. Epub , 2024 Apr 18. PMID:38634647<ref>PMID:38634647</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8vyc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermobifida fusca YX]]
[[Category: Choi B]]
[[Category: Link AJ]]