5L44

Structure of K-26-DCP in complex with the K-26 tripeptide

Summary for 5L44

• Entry DOI: 10.2210/pdb5l44/pdb
• Descriptor: K-26 dipeptidyl carboxypeptidase, ZINC ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: dipeptidyl carboxypeptidase, metalloprotease, k-26 tripeptide, angiotensin-1 converting enzyme, hydrolase
• Biological source: Astrosporangium hypotensionis K-26
• Total number of polymer chains: 2
• Total formula weight: 154682.66

Authors

Masuyer, G.,Acharya, K.R.,Kramer, G.J.,Bachmann, B.O. (deposition date: 2016-05-24, release date: 2016-10-26, Last modification date: 2024-01-10)

Primary citation

Masuyer, G.,Cozier, G.E.,Kramer, G.J.,Bachmann, B.O.,Acharya, K.R.
Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor.
FEBS J., 283:4357-4369, 2016

PubMed 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.

PubMed: 27754586
DOI: 10.1111/febs.13928

Experimental method

X-RAY DIFFRACTION (1.75 Å)