2z37
From Proteopedia
(New page: 200px<br /><applet load="2z37" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z37, resolution 1.530Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | Brassica juncea chitinase is an endo-acting, pathogenesis-related protein | + | Brassica juncea chitinase is an endo-acting, pathogenesis-related protein that is classified into glycoside hydrolase family 19, with highest homology (50-60%) in its catalytic domain to class I plant chitinases. Here we report X-ray structures of the chitinase catalytic domain from wild-type (apo, as well as with chloride ions bound) and a Glu234Ala mutant enzyme, solved by molecular replacement and refined at 1.53, 1.8 and 1.7 A resolution, respectively. Confirming our earlier mutagenesis studies, the active-site residues are identified as Glu212 and Glu234. Glu212 is believed to be the catalytic acid in the reaction, whereas Glu234 is thought to have a dual role, both activating a water molecule in its attack on the anomeric carbon, and stabilizing the charged intermediate. The molecules in the various structures differ significantly in the conformation of a number of loops that border the active-site cleft. The differences suggest an opening and closing of the enzyme during the catalytic cycle. Chitin is expected to dock first near Glu212, which will protonate it. Conformational changes then bring Glu234 closer, allowing it to assist in the following steps. These observations provide important insights into catalysis in family 19 chitinases. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Bergfors, T.]] | [[Category: Bergfors, T.]] | ||
[[Category: Berglund, G.]] | [[Category: Berglund, G.]] | ||
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
[[Category: Ubhayasekera, W.]] | [[Category: Ubhayasekera, W.]] | ||
[[Category: chitinase]] | [[Category: chitinase]] | ||
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[[Category: family 19]] | [[Category: family 19]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:59:48 2008'' |
Revision as of 16:59, 21 February 2008
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Crystal structure of Brassica juncea chitinase catalytic module (Bjchi3)
Overview
Brassica juncea chitinase is an endo-acting, pathogenesis-related protein that is classified into glycoside hydrolase family 19, with highest homology (50-60%) in its catalytic domain to class I plant chitinases. Here we report X-ray structures of the chitinase catalytic domain from wild-type (apo, as well as with chloride ions bound) and a Glu234Ala mutant enzyme, solved by molecular replacement and refined at 1.53, 1.8 and 1.7 A resolution, respectively. Confirming our earlier mutagenesis studies, the active-site residues are identified as Glu212 and Glu234. Glu212 is believed to be the catalytic acid in the reaction, whereas Glu234 is thought to have a dual role, both activating a water molecule in its attack on the anomeric carbon, and stabilizing the charged intermediate. The molecules in the various structures differ significantly in the conformation of a number of loops that border the active-site cleft. The differences suggest an opening and closing of the enzyme during the catalytic cycle. Chitin is expected to dock first near Glu212, which will protonate it. Conformational changes then bring Glu234 closer, allowing it to assist in the following steps. These observations provide important insights into catalysis in family 19 chitinases.
About this Structure
2Z37 is a Single protein structure of sequence from Brassica juncea. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops., Ubhayasekera W, Tang CM, Ho SW, Berglund G, Bergfors T, Chye ML, Mowbray SL, FEBS J. 2007 Jul;274(14):3695-703. Epub 2007 Jul 2. PMID:17608716
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