Structural highlights
Function
ATXE2_ASTEC Lasso peptide isopeptidase that specifically hydrolyzes Astexin-2 and Astexin-3, converting them to linear peptides (PubMed:23862624). Has only a few specific contacts with subrates, because it recognizes Astexin knotted structure (principally the loop structure) (PubMed:26534965, PubMed:27998080). Its binding to lasso peptides opens them to expose the isopeptide bonds for hydrolysis (PubMed:27998080).[1] [2] [3]
References
- ↑ Maksimov MO, Link AJ. Discovery and Characterization of an Isopeptidase that Linearizes Lasso Peptides. J Am Chem Soc. 2013 Jul 17. PMID:23862624 doi:10.1021/ja4054256
- ↑ 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
- ↑ Chekan JR, Koos JD, Zong C, Maksimov MO, Link AJ, Nair SK. Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates. J Am Chem Soc. 2016 Dec 21;138(50):16452-16458. doi: 10.1021/jacs.6b10389. Epub, 2016 Dec 7. PMID:27998080 doi:http://dx.doi.org/10.1021/jacs.6b10389