2n6u | pdb_00002n6u

Solution study of Astexin2-dC4

spinqualitylabelsall models 2n6u, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n6u is a 1 chain structure with sequence from Astec. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2n6v Gene: Astex_2448 (ASTEC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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