2gwc

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[[Image:2gwc.gif|left|200px]]<br /><applet load="2gwc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2gwc.gif|left|200px]]
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caption="2gwc, resolution 2.18&Aring;" />
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'''Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue'''<br />
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{{Structure
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|PDB= 2gwc |SIZE=350|CAPTION= <scene name='initialview01'>2gwc</scene>, resolution 2.18&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=BSC:(S)-2-AMINO-4-(AMINO-BUTYLHYDROSULFINYL)BUTANOIC ACID'>BSC</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate--cysteine_ligase Glutamate--cysteine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.2 6.3.2.2]
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|GENE= GSH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3707 Brassica juncea])
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}}
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'''Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2GWC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=BSC:'>BSC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--cysteine_ligase Glutamate--cysteine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.2 6.3.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWC OCA].
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2GWC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWC OCA].
==Reference==
==Reference==
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Structural basis for the redox control of plant glutamate cysteine ligase., Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K, J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16766527 16766527]
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Structural basis for the redox control of plant glutamate cysteine ligase., Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K, J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16766527 16766527]
[[Category: Brassica juncea]]
[[Category: Brassica juncea]]
[[Category: Glutamate--cysteine ligase]]
[[Category: Glutamate--cysteine ligase]]
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[[Category: MG]]
[[Category: MG]]
[[Category: beta-hairpin]]
[[Category: beta-hairpin]]
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[[Category: disulfide bridges]]
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[[Category: disulfide bridge]]
[[Category: glutathione biosynthesis]]
[[Category: glutathione biosynthesis]]
[[Category: redox regulation]]
[[Category: redox regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:09:56 2008''

Revision as of 15:09, 20 March 2008


PDB ID 2gwc

Drag the structure with the mouse to rotate
, resolution 2.18Å
Ligands: and
Gene: GSH1 (Brassica juncea)
Activity: Glutamate--cysteine ligase, with EC number 6.3.2.2
Coordinates: save as pdb, mmCIF, xml



Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue


Overview

Glutathione (GSH) plays a crucial role in plant metabolism and stress response. The rate-limiting step in the biosynthesis of GSH is catalyzed by glutamate cysteine ligase (GCL) the activity of which is tightly regulated. The regulation of plant GCLs is poorly understood. The crystal structure of substrate-bound GCL from Brassica juncea at 2.1-A resolution reveals a plant-unique regulatory mechanism based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of B. juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of B. juncea GCL that is associated with a significant inactivation of the enzyme. These regulatory events provide a molecular link between high GSH levels in the plant cell and associated down-regulation of its biosynthesis. Furthermore, known mutations in the Arabidopsis GCL gene affect residues in the close proximity of the active site and thus explain the decreased GSH levels in mutant plants. In particular, the mutation in rax1-1 plants causes impaired binding of cysteine.

About this Structure

2GWC is a Single protein structure of sequence from Brassica juncea. Full crystallographic information is available from OCA.

Reference

Structural basis for the redox control of plant glutamate cysteine ligase., Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K, J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527

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