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Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology. (T. Alwyn Jones)
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2007 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 274, no 14, 3695-3703 p.Article in journal (Refereed) Published
Abstract [en]

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 Å 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.

Place, publisher, year, edition, pages
2007. Vol. 274, no 14, 3695-3703 p.
Keyword [en]
Brassica juncea, chitinase, conformational changes, endochitinase, family 19
National Category
Biological Sciences
URN: urn:nbn:se:uu:diva-14450DOI: 10.1111/j.1742-4658.2007.05906.xISI: 000247904900020PubMedID: 17608716OAI: oai:DiVA.org:uu-14450DiVA: diva2:42220
Available from: 2008-01-30 Created: 2008-01-30 Last updated: 2015-03-31Bibliographically approved

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