2f1k
From Proteopedia
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[[Image:2f1k.gif|left|200px]] | [[Image:2f1k.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2f1k| PDB=2f1k | SCENE= }} | |
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'''Crystal structure of Synechocystis arogenate dehydrogenase''' | '''Crystal structure of Synechocystis arogenate dehydrogenase''' | ||
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[[Category: Rippert, P.]] | [[Category: Rippert, P.]] | ||
[[Category: Seux, M.]] | [[Category: Seux, M.]] | ||
| - | [[Category: | + | [[Category: Arogenate/prephenate dehydrogenase]] |
| - | [[Category: | + | [[Category: Tyrosine synthesis]] |
| - | [[Category: | + | [[Category: X-ray crystallography structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:21:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:21, 4 May 2008
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.. 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 Page seeded by OCA on Sun May 4 03:21:16 2008
