Crystal structure of a peptidyl‐dipeptidase K‐26‐DCP from Actinomycete in complex with its natural inhibitor
Copyright policy )Crystal structure of a peptidyl‐dipeptidase K‐26‐DCP from Actinomycete in complex with its natural inhibitor
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.DatabaseStructural data are available in the PDB under the accession numbers 5L43 and 5L44.
- University of Bath
- Vanderbilt University United States
- Stockholm University Sweden
- University of Toronto Canada
- University of Bath United Kingdom
Models, Molecular, Sequence Homology, Amino Acid, Angiotensin-Converting Enzyme Inhibitors, Original Articles, Peptidyl-Dipeptidase A, Crystallography, X-Ray, Actinobacteria, Bacterial Proteins, Protein Domains, Endopeptidases, Humans, Amino Acid Sequence, Enzyme Inhibitors, Databases, Protein, Oligopeptides, Protein Binding
Models, Molecular, Sequence Homology, Amino Acid, Angiotensin-Converting Enzyme Inhibitors, Original Articles, Peptidyl-Dipeptidase A, Crystallography, X-Ray, Actinobacteria, Bacterial Proteins, Protein Domains, Endopeptidases, Humans, Amino Acid Sequence, Enzyme Inhibitors, Databases, Protein, Oligopeptides, Protein Binding
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