1dxj

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Image:1dxj.gif

1dxj, resolution 1.8Å

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STRUCTURE OF THE CHITINASE FROM JACK BEAN

Overview

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.

About this Structure

1DXJ is a Single protein structure of sequence from Canavalia ensiformis with as ligand. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.

Reference

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

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