We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2f1k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2f1k |SIZE=350|CAPTION= <scene name='initialview01'>2f1k</scene>, resolution 1.55&Aring;
|PDB= 2f1k |SIZE=350|CAPTION= <scene name='initialview01'>2f1k</scene>, resolution 1.55&Aring;
|SITE=
|SITE=
-
|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>
+
|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
-
|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]
+
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= D90910.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
|GENE= D90910.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1k OCA], [http://www.ebi.ac.uk/pdbsum/2f1k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1k RCSB]</span>
}}
}}
Line 30: Line 33:
[[Category: Rippert, P.]]
[[Category: Rippert, P.]]
[[Category: Seux, M.]]
[[Category: Seux, M.]]
-
[[Category: NAP]]
 
-
[[Category: TRS]]
 
[[Category: arogenate/prephenate dehydrogenase]]
[[Category: arogenate/prephenate dehydrogenase]]
[[Category: tyrosine synthesis]]
[[Category: tyrosine synthesis]]
[[Category: x-ray crystallography structure]]
[[Category: x-ray crystallography structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:47:03 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:38 2008''

Revision as of 23:56, 30 March 2008


PDB ID 2f1k

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands: , , ,
Gene: D90910.1 (Synechocystis sp.)
Activity: Arogenate dehydrogenase, with EC number 1.3.1.43
Resources: FirstGlance, OCA, PDBsum, RCSB
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

Page seeded by OCA on Mon Mar 31 02:56:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools