The structure of jack bean chitinase was solved at 1.8 A 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(epsilon1) and Thr119 O(gamma) at a distance of 3.0 and 2.8 A, respectively. The model is in accordance with the observed inversion mechanism.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The structure of jack bean chitinase was solved at 1.8 A 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(epsilon1) and Thr119 O(gamma) at a distance of 3.0 and 2.8 A, respectively. The model is in accordance with the observed inversion mechanism.
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| skos:exactMatch | |
| uniprot:name |
Acta Crystallogr. D,
Acta Crystallogr. D Biol. Crystallogr.
|
| uniprot:author |
Hahn M.,
Hennig M.,
Hohne W.,
Schlesier B.
|
| uniprot:date |
2000
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| uniprot:pages |
1096-1099
|
| uniprot:title |
Structure of jack bean chitinase.
|
| uniprot:volume |
56
|
| dc-term:identifier |
doi:10.1107/S090744490000857X
|