1gsn
From Proteopedia
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| - | [[Image:1gsn.gif|left|200px]] | + | [[Image:1gsn.gif|left|200px]] |
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| - | '''HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE''' | + | {{Structure |
| + | |PDB= 1gsn |SIZE=350|CAPTION= <scene name='initialview01'>1gsn</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GSN is a [ | + | 1GSN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSN OCA]. |
==Reference== | ==Reference== | ||
| - | Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers., Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA, Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:[http:// | + | Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers., Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA, Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9546215 9546215] |
[[Category: Glutathione-disulfide reductase]] | [[Category: Glutathione-disulfide reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: sulfhydryl oxidation]] | [[Category: sulfhydryl oxidation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:23 2008'' |
Revision as of 09:27, 20 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Glutathione-disulfide reductase, with EC number 1.8.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE
Contents |
Overview
Nitric oxide (NO) is a pluripotent regulatory molecule, yet the molecular mechanisms by which it exerts its effects are largely unknown. Few physiologic target molecules of NO have been identified, and even for these, the modifications caused by NO remain uncharacterized. Human glutathione reductase (hGR), a central enzyme of cellular antioxidant defense, is inhibited by S-nitrosoglutathione (GSNO) and by diglutathionyl-dinitroso-iron (DNIC-[GSH]2), two in vivo transport forms of NO. Here, crystal structures of hGR inactivated by GSNO and DNIC-[GSH]2 at 1.7 A resolution provide the first picture of enzyme inactivation by NO-carriers: in GSNO-modified hGR, the active site residue Cys 63 is oxidized to an unusually stable cysteine sulfenic acid (R-SOH), whereas modification with DNIC-[GSH]2 oxidizes Cys 63 to a cysteine sulfinic acid (R-SO2H). Our results illustrate that various forms of NO can mediate distinct chemistry, and that sulfhydryl oxidation must be considered as a major mechanism of NO action.
Disease
Known diseases associated with this structure: Hemolytic anemia due to glutathione reductase deficiency OMIM:[138300], Mental retardation, autosomal recessive, 6 OMIM:[138244]
About this Structure
1GSN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers., Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA, Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:9546215
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