Structure of jack bean chitinase

被引：51

作者：

Hahn, M

Hennig, M

Schlesier, B

Höhne, W

机构：

[1] Humboldt Univ, Inst Biochem, Charite, D-10117 Berlin, Germany

[2] Hoffmann La Roche AG, Pharmaceut Res 65 308, CH-4070 Basel, Switzerland

[3] IPK Gatersleben, Inst Pflanzengenet & Kulturpflanzenforsch, D-06466 Gatersleben, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷

关键词：

D O I：

10.1107/S090744490000857X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of jack bean chitinase was solved at 1.8 Angstrom resolution by molecular replacement. It is an alpha-helical protein with three disulfide bridges. The active site is related in structure to animal and viral lysozymes. However, unlike in lysozyme, the architecture of the active site suggests a single-step cleavage. According to this mechanism, Glu68 is the proton donor and Glu90 assists in the reaction by moving towards the substrate and recruiting a water molecule that acts as the nucleophile. In this model, a water molecule was found in contact with Glu90 O-epsilon 1 and Thr119 O-gamma at a distance of 3.0 and 2.8 Angstrom, respectively. The model is in accordance with the observed inversion mechanism.

引用

页码：1096 / 1099

页数：4

共 26 条

[1] The role of enzyme distortion in the single displacement mechanism of family 19 chitinases [J].