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

DOI: 10.1111/febs.13928 DOI Help

Authors: Geoffrey Masuyer (Department of Biology and Biochemistry, University of Bath) , Gyles E. Cozier (Department of Biology and Biochemistry, University of Bath) , Glenna J. Kramer (Department of Chemistry, Vanderbilt University) , Brian O. Bachmann (Department of Chemistry, Vanderbilt University) , Ravi Acharya (Department of Biology and Biochemistry, University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Febs Journal

State: Published (Approved)
Published: November 2016
Diamond Proposal Number(s): 8922

Open Access Open Access

Abstract: 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.

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

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