X‐ray crystallographic structure of a papain‐leupeptin complex

FEBS Letters

Harlos, Karl¹  Crawford, Catherine¹  Schröder, Ewald¹  Phillips, Christopher¹  Garman, Elspeth¹ 

[1] University of Oxford, Laboratory of Molecular Biophysics, The Rex Richards Building, South Parks Road, Oxford, OX1 3QU, UK

关键词: Leupeptin;    Papain;    Enzyme-inhibitor complex;    Oxyanion hole;    Hemithioacetal;    X-ray crystallography;   

DOI  :  10.1016/0014-5793(93)81128-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The three-dimensional structure of the papain-leupeptin complex has been determined by X-ray crystallography to a resolution of 2.1 Å (overall R-factor = 19.8%). The structure indicates that: (i) leupeptin contacts the S subsites of the papain active site and not the S'subsites; (ii) the ‘carbonyl’ carbon atom of the inhibitor is covalently bound by the Cys-25 sulphur atom of papain and is tetrahedrally coordinated; (iii) the ‘carbonyl’ oxygen atom of the inhibitor faces the oxyanion hole and makes hydrogen bond contacts with Gln-19 and Cys-25.

【 授权许可】

Unknown