2m8f: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2m8f is ~~ON HOLD until Paper~~ Publication

==Structure of lasso peptide astexin3==

== Structural highlights ==

<table><tr><td colspan='2'>[[2m8f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Asticcacaulis_excentricus_CB_48 Asticcacaulis excentricus CB 48]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M8F FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2m8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8f OCA], [https://pdbe.org/2m8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m8f RCSB], [https://www.ebi.ac.uk/pdbsum/2m8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8f ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Lasso peptides are a class of ribosomally-derived natural products with diverse bioactivities. The characteristic threaded lasso structure in these peptides derives from an isopeptide bond attaching the N-terminus of the peptide to an acidic sidechain. Here we describe the heterologous expression of a lasso peptide gene cluster encoding two lasso peptides, astexin-2 and astexin-3 and solve the solution structure of astexin-3. This cluster also encodes an enzyme annotated as a protease. We show that this enzyme, AtxE2, is a lasso peptide isopeptidase that specifically hydrolyzes astexins-2 and -3 converting them to linear peptides. Astexin-3 is highly thermostable and resists unthreading after extensive heat treatment. In contrast, astexin-2 unthreads upon heat treatment. AtxE2 has no activity toward unthreaded astexin-2 demonstrating that this isopeptidase must recognize a knotted structure in order to function. We also use this isopeptidase as a tool to study evolutionary relationships between lasso peptide gene clusters.

~~Authors:~~ Maksimov, M.~~O., Link, A~~.

Discovery and Characterization of an Isopeptidase that Linearizes Lasso Peptides.,Maksimov MO, Link AJ J Am Chem Soc. 2013 Jul 17. PMID:23862624<ref>PMID:23862624</ref>

~~Description~~: ~~Structure of lasso peptide astexin3~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Asticcacaulis excentricus CB 48]]

[[Category: Large Structures]]

[[Category: Link A]]

[[Category: Maksimov MO]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2m8f is ON HOLD  until Paper Publication
+==Structure of lasso peptide astexin3==
+<StructureSection load='2m8f' size='340' side='right'caption='[[2m8f]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2m8f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Asticcacaulis_excentricus_CB_48 Asticcacaulis excentricus CB 48]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M8F FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2m8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8f OCA], [https://pdbe.org/2m8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m8f RCSB], [https://www.ebi.ac.uk/pdbsum/2m8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8f ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Lasso peptides are a class of ribosomally-derived natural products with diverse bioactivities. The characteristic threaded lasso structure in these peptides derives from an isopeptide bond attaching the N-terminus of the peptide to an acidic sidechain. Here we describe the heterologous expression of a lasso peptide gene cluster encoding two lasso peptides, astexin-2 and astexin-3 and solve the solution structure of astexin-3. This cluster also encodes an enzyme annotated as a protease. We show that this enzyme, AtxE2, is a lasso peptide isopeptidase that specifically hydrolyzes astexins-2 and -3 converting them to linear peptides. Astexin-3 is highly thermostable and resists unthreading after extensive heat treatment. In contrast, astexin-2 unthreads upon heat treatment. AtxE2 has no activity toward unthreaded astexin-2 demonstrating that this isopeptidase must recognize a knotted structure in order to function. We also use this isopeptidase as a tool to study evolutionary relationships between lasso peptide gene clusters.
-Authors: Maksimov, M.O., Link, A.
+Discovery and Characterization of an Isopeptidase that Linearizes Lasso Peptides.,Maksimov MO, Link AJ J Am Chem Soc. 2013 Jul 17. PMID:23862624<ref>PMID:23862624</ref>
-Description: Structure of lasso peptide astexin3
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2m8f" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Asticcacaulis excentricus CB 48]]
+[[Category: Large Structures]]
+[[Category: Link A]]
+[[Category: Maksimov MO]]