1dxj
From Proteopedia
(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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| - | [[Image:1dxj.gif|left|200px]]<br /><applet load="1dxj" size=" | + | [[Image:1dxj.gif|left|200px]]<br /><applet load="1dxj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dxj, resolution 1.8Å" /> | caption="1dxj, resolution 1.8Å" /> | ||
'''STRUCTURE OF THE CHITINASE FROM JACK BEAN'''<br /> | '''STRUCTURE OF THE CHITINASE FROM JACK BEAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of jack bean chitinase was solved at 1.8 A resolution by | + | 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== | ==About this Structure== | ||
| - | 1DXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http:// | + | 1DXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:37 2008'' |
Revision as of 10:21, 21 February 2008
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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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