Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor

Geoffrey Masuyer, Gyles E. Cozier, Glenna J. Kramer, Brian O. Bachmann, K. Ravi Acharya

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Several soil-derived Actinobacteria produce secondary metabolites that are proven specific and potent inhibitors of the human angiotensin-I-converting enzyme (ACE), a key target for the modulation of hypertension through its role in the renin–angiotensin–aldosterone system. K-26-DCP is a zinc dipeptidyl carboxypeptidase (DCP) produced by Astrosporangium hypotensionis, and an ancestral homologue of ACE. Here we report the high-resolution crystal structures of K-26-DCP and of its complex with the natural microbial tripeptide product K-26. The experimental results provide the structural basis for better understanding the specificity of K-26 for human ACE over bacterial DCPs. Database: Structural data are available in the PDB under the accession numbers 5L43 and 5L44.

Original languageEnglish
Pages (from-to)4357-4369
Number of pages13
JournalFEBS Journal
Issue number23
Publication statusPublished - 1 Dec 2016


  • angiotensin-I-converting enzyme
  • dipeptidyl carboxypeptidase
  • K-26 tripeptide
  • metalloprotease


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