1vdc: Difference between revisions

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[[Image:1vdc.gif|left|200px]]<br /><applet load="1vdc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1vdc.gif|left|200px]]
caption="1vdc, resolution 2.5&Aring;" />
 
'''STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE'''<br />
{{Structure
|PDB= 1vdc |SIZE=350|CAPTION= <scene name='initialview01'>1vdc</scene>, resolution 2.5&Aring;
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> and <scene name='pdbsite=FAD:Fad+Binding+Site'>FAD</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_1.8.1.9 Transferred entry: 1.8.1.9], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.4.5 1.6.4.5]
|GENE= ATTHIREDB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
}}
 
'''STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1VDC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_1.8.1.9 Transferred entry: 1.8.1.9], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.4.5 1.6.4.5] Known structural/functional Sites: <scene name='pdbsite=ACT:Active+Site'>ACT</scene> and <scene name='pdbsite=FAD:Fad+Binding+Site'>FAD</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDC OCA].  
1VDC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDC OCA].  


==Reference==
==Reference==
Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution., Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H, J Mol Biol. 1996 Dec 20;264(5):1044-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9000629 9000629]
Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution., Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H, J Mol Biol. 1996 Dec 20;264(5):1044-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9000629 9000629]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thioredoxin reductase]]
[[Category: thioredoxin reductase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:11 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:03 2008''

Revision as of 15:44, 20 March 2008

File:1vdc.gif


PDB ID 1vdc

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites: and
Ligands: and
Gene: ATTHIREDB (Arabidopsis thaliana)
Activity: Transferred entry: 1.8.1.9, with EC number 1.6.4.5
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE


OverviewOverview

Thioredoxin exists in all organisms and is responsible for the hydrogen transfer to important enzymes for ribonucleotide reduction and the reduction of methionine sulphoxide and sulphate. Thioredoxins have also been shown to regulate enzyme activity in plants and are also involved in the regulation of transcription factors and several other regulatory activities. Thioredoxin is reduced by the flavoenzyme thioredoxin reductase using NADPH. We have now determined the first structure of a eukaryotic thioredoxin reductase, from the plant Arabidopsis thaliana, at 2.5 A resolution. The dimeric A. thaliana thioredoxin reductase is structurally similar to that of the Escherichia coli enzyme, and most differences occur in the loops. Because the plant and E. coli enzymes have the same architecture, with the same dimeric structure and the same position of the redox active disulphide bond, a similar mechanism that involves very large domain rotations is likely for the two enzymes. The subunit is divided into two domains, one that binds FAD and one that binds NADPH. The relative positions of the domains in A. thaliana thioredoxin reductase differ from those of the E. coli reductase. When the FAD domains are superimposed, the NADPH domain of A. thaliana thioredoxin reductase must be rotated by 8 degrees to superimpose on the corresponding domain of the E. coli enzyme. The domain rotation we now observe is much smaller than necessary for the thioredoxin reduction cycle.

About this StructureAbout this Structure

1VDC is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution., Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H, J Mol Biol. 1996 Dec 20;264(5):1044-57. PMID:9000629

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