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2f1k

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[[Image:2f1k.gif|left|200px]]<br /><applet load="2f1k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2f1k.gif|left|200px]]
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caption="2f1k, resolution 1.55&Aring;" />
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'''Crystal structure of Synechocystis arogenate dehydrogenase'''<br />
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{{Structure
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|PDB= 2f1k |SIZE=350|CAPTION= <scene name='initialview01'>2f1k</scene>, resolution 1.55&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Arogenate_dehydrogenase Arogenate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.43 1.3.1.43]
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|GENE= D90910.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
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}}
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'''Crystal structure of Synechocystis arogenate dehydrogenase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2F1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arogenate_dehydrogenase Arogenate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.43 1.3.1.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1K OCA].
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2F1K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1K OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16615917 16615917]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16615917 16615917]
[[Category: Arogenate dehydrogenase]]
[[Category: Arogenate dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: x-ray crystallography structure]]
[[Category: x-ray crystallography structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:47:03 2008''

Revision as of 14:47, 20 March 2008

Image:2f1k.gif


PDB ID 2f1k

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands: and
Gene: D90910.1 (Synechocystis sp.)
Activity: Arogenate dehydrogenase, with EC number 1.3.1.43
Coordinates: save as pdb, mmCIF, xml



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

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