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2f1k

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(New page: 200px<br /><applet load="2f1k" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f1k, resolution 1.55&Aring;" /> '''Crystal structure of...)
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Revision as of 17:25, 29 January 2008

Image:2f1k.gif

2f1k, resolution 1.55Å

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Crystal structure of Synechocystis arogenate dehydrogenase

Overview

The extreme diversity in substrate specificity, and in the regulation, mechanism of arogenate/prephenate dehydrogenase enzymes in nature, makes a, comparative structural study of these enzymes of great interest. We report, here on the biochemical and structural characterization of arogenate, dehydrogenase from Synechocystis sp. (TyrAsy). This work paves the way for, the understanding of the structural determinants leading to diversity in, substrate specificity, and of the regulation mechanisms of, arogenate/prephenate dehydrogenases. The overall structure of TyrAsy in, complex with NADP was refined to 1.6 A. The asymmetric unit contains two, TyrAsy homodimers, with each monomer consisting of a nucleotide binding, N-terminal domain and a particularly unique alpha-helical C-terminal, dimerization domain. The substrate arogenate was modeled into the active, site. The model of the ternary complex enzyme-NADP-arogenate nicely, reveals at the atomic level the concerted mechanism of the, arogenate/prephenate dehydrogenase reaction.

About this Structure

2F1K is a Single protein structure of sequence from Synechocystis sp. with and as ligands. Active as Arogenate dehydrogenase, with EC number 1.3.1.43 Full crystallographic information is available from OCA.

Reference

Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction., Legrand P, Dumas R, Seux M, Rippert P, Ravelli R, Ferrer JL, Matringe M, Structure. 2006 Apr;14(4):767-76. PMID:16615917

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