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    FEBS Lett. 2003 Mar 13;538(1-3):65-70.

    Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril.

    Source

    Department of Biological Science, Korea Advanced Institute of Science and Technology, 373-1 Kusong-dong, Yusong-gu, Daejeon, South Korea.

    Abstract

    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.

    PMID:
    12633854
    [PubMed - indexed for MEDLINE]

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