2oxb
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(New page: 200px<br /><applet load="2oxb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oxb, resolution 2.60Å" /> '''Crystal structure of...)
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Revision as of 08:49, 23 January 2008
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Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose
Overview
In the present study, we report on the X-ray crystallographic structure of, a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall, invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This, structure was solved to reveal the features of sugar binding in the, catalytic pocket. However, as demonstrated by the X-ray structure the, sugar binding and the catalytic pocket arrangement is significantly, altered as compared with what was expected based on previous X-ray, structures on GH-J clan enzymes. We performed a series of docking and, molecular dynamics simulations on various derivatives of AtcwINV1 to, reveal the reasons behind this modified sugar binding. Our results, demonstrate that the E203Q mutation introduced into the catalytic pocket, triggers conformational changes that alter the wild type substrate, binding. In addition, this study also reveals the putative productive, sucrose binding modus in the wild type enzyme. Proteins 2007. (c) 2007, Wiley-Liss, Inc.
About this Structure
2OXB is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Active as Beta-fructofuranosidase, with EC number 3.2.1.26 Full crystallographic information is available from OCA.
Reference
An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study., Matrai J, Lammens W, Jonckheer A, Le Roy K, Rabijns A, Van den Ende W, De Maeyer M, Proteins. 2007 Oct 26;. PMID:17963237
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