Structural highlights
Function
O81934_CANEN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of jack bean chitinase.,Hahn M, Hennig M, Schlesier B, Hohne W Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1096-9. PMID:10957628[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hahn M, Hennig M, Schlesier B, Hohne W. Structure of jack bean chitinase. Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1096-9. PMID:10957628