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1dxj
From Proteopedia
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(New page: 200px<br /><applet load="1dxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dxj, resolution 1.8Å" /> '''STRUCTURE OF THE CHIT...)
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Revision as of 01:40, 25 November 2007
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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 SO4 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
Page seeded by OCA on Sun Nov 25 03:48:29 2007
