2f1k: Difference between revisions

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[[Image:2f1k.~~gif~~|left|200px]]

[[Image:2f1k.png|left|200px]]

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~~'''~~Crystal structure of Synechocystis arogenate dehydrogenase~~'''~~

===Crystal structure of Synechocystis arogenate dehydrogenase===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16615917}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16615917 is the PubMed ID number.

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==About this Structure==

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[[Category: Tyrosine synthesis]]

[[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 Mon Jul 28 08:22:12 2008''

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-[[Image:2f1k.gif|left|200px]]
+{{Seed}}
+[[Image:2f1k.png|left|200px]]
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 {{STRUCTURE_2f1k|  PDB=2f1k  |  SCENE=  }}
-'''Crystal structure of Synechocystis arogenate dehydrogenase'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16615917}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16615917 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16615917}}
 ==About this Structure==
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 [[Category: Tyrosine synthesis]]
 [[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 Mon Jul 28 08:22:12 2008''