1J37

Crystal Structure of Drosophila AnCE

Summary for 1J37

• Entry DOI: 10.2210/pdb1j37/pdb
• Related: 1J36 1J38
• Descriptor: angiotensin converting enzyme, ZINC ION, L-CAPTOPRIL (3 entities in total)
• Functional Keywords: angiotensin, hydrolase
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Secreted, extracellular space: Q10714
• Total number of polymer chains: 2
• Total formula weight: 141445.70

Authors

Kim, H.M.,Shin, D.R.,Yoo, O.J.,Lee, H.,Lee, J.-O. (deposition date: 2003-01-20, release date: 2003-07-20, Last modification date: 2023-12-27)

Primary citation

Kim, H.M.,Shin, D.R.,Yoo, O.J.,Lee, H.,Lee, J.-O.
Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril
Febs Lett., 538:65-70, 2003

PubMed 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.

PubMed: 12633854
DOI: 10.1016/S0014-5793(03)00128-5

Experimental method

X-RAY DIFFRACTION (2.4 Å)