|1j37, resolution 2.40Å ()|
Crystal Structure of Drosophila AnCE
Angiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosophila homolog of ACE, with and without bound inhibitors to 2.4 A resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif.
Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril., Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO, FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
[ACE_DROME] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.
About this Structure
- Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO. Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril. FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854