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2m8f

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(New page: '''Unreleased structure''' The entry 2m8f is ON HOLD until Paper Publication Authors: Maksimov, M.O., Link, A. Description: Structure of lasso peptide astexin3)
Current revision (06:27, 2 March 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2m8f is ON HOLD until Paper Publication
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==Structure of lasso peptide astexin3==
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<StructureSection load='2m8f' size='340' side='right'caption='[[2m8f]]' scene=''>
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== Structural highlights ==
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<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>
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASTX3_ASTEC ASTX3_ASTEC] Shows weak antimicrobial activity against its phylogenetic relative Caulobacter crescentus. Does not show activity against other bacteria tested (E.coli, Vibrio sp, Burkhoderia thailandensis, and Salmonella newport).[UniProtKB:E8RMD3]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Maksimov, M.O., Link, A.
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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>
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Description: Structure of lasso peptide astexin3
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2m8f" 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: Asticcacaulis excentricus CB 48]]
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[[Category: Large Structures]]
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[[Category: Link A]]
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[[Category: Maksimov MO]]

Current revision

Structure of lasso peptide astexin3

PDB ID 2m8f

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