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| | ==Solution study of Astexin2-dC4== | | ==Solution study of Astexin2-dC4== |
| - | <StructureSection load='2n6u' size='340' side='right' caption='[[2n6u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2n6u' size='340' side='right'caption='[[2n6u]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n6u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Astec Astec]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N6U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N6U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n6u]] 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=2N6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N6U FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n6v|2n6v]]</td></tr> | + | </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=2n6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6u OCA], [https://pdbe.org/2n6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6u RCSB], [https://www.ebi.ac.uk/pdbsum/2n6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6u ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Astex_2448 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573065 ASTEC])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6u OCA], [http://pdbe.org/2n6u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n6u RCSB], [http://www.ebi.ac.uk/pdbsum/2n6u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASTX2_ASTEC ASTX2_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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Astec]] | + | [[Category: Asticcacaulis excentricus CB 48]] |
| - | [[Category: Link, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Maksimov, M O]] | + | [[Category: Link A]] |
| - | [[Category: Lasso peptide]] | + | [[Category: Maksimov MO]] |
| - | [[Category: Unknown function]]
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| Structural highlights
Function
ASTX2_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]
Publication Abstract from PubMed
Lasso peptide isopeptidase is an enzyme that specifically hydrolyzes the isopeptide bond of lasso peptides, rendering these peptides linear. In order to carry out a detailed structure-activity analysis of the lasso peptide isopeptidase AtxE2 from Asticcacaulis excentricus, we solved NMR structures of its substrates astexin-2 and astexin-3. Using in vitro enzyme assays, we show that the C-terminal tail portion of these peptides is dispensable with regards to isopeptidase activity. A collection of astexin-2 and astexin-3 variants with alanine substitutions at each position within the ring and the loop was constructed, and we showed that all of these peptides except for one were cleaved by the isopeptidase. Thus, much like the lasso peptide biosynthetic enzymes, lasso peptide isopeptidase has broad substrate specificity. Quantitative analysis of the cleavage reactions indicated that alanine substitutions in loop positions of these peptides led to reduce cleavage, suggesting that the loop is serving as a recognition element for the isopeptidase.
Elucidating the Specificity Determinants of the AtxE2 Lasso Peptide Isopeptidase.,Maksimov MO, Koos JD, Zong C, Lisko B, Link AJ J Biol Chem. 2015 Nov 3. pii: jbc.M115.694083. PMID:26534965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maksimov MO, Koos JD, Zong C, Lisko B, Link AJ. Elucidating the Specificity Determinants of the AtxE2 Lasso Peptide Isopeptidase. J Biol Chem. 2015 Nov 3. pii: jbc.M115.694083. PMID:26534965 doi:http://dx.doi.org/10.1074/jbc.M115.694083
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