1J37

Crystal Structure of Drosophila AnCE

1J37 の概要

• エントリーDOI: 10.2210/pdb1j37/pdb
• 関連するPDBエントリー: 1J36 1J38
• 分子名称: angiotensin converting enzyme, ZINC ION, L-CAPTOPRIL (3 entities in total)
• 機能のキーワード: angiotensin, hydrolase
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Secreted, extracellular space: Q10714
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141445.70

構造登録者

Kim, H.M.,Shin, D.R.,Yoo, O.J.,Lee, H.,Lee, J.-O. (登録日: 2003-01-20, 公開日: 2003-07-20, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)