2f1k
From Proteopedia
(New page: 200px<br /><applet load="2f1k" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f1k, resolution 1.55Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | The extreme diversity in substrate specificity, and in the regulation | + | 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== | ==About this Structure== | ||
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[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
[[Category: Dumas, R.]] | [[Category: Dumas, R.]] | ||
| - | [[Category: Ferrer, J | + | [[Category: Ferrer, J L.]] |
[[Category: Legrand, P.]] | [[Category: Legrand, P.]] | ||
[[Category: Matringe, M.]] | [[Category: Matringe, M.]] | ||
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[[Category: x-ray crystallography structure]] | [[Category: x-ray crystallography structure]] | ||
| - | ''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 17:16:45 2008'' |
Revision as of 15:16, 21 February 2008
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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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