2rab
From Proteopedia
(New page: 200px<br /><applet load="2rab" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rab, resolution 2.50Å" /> '''Structure of glutath...) |
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| - | [[Image:2rab.jpg|left|200px]] | + | [[Image:2rab.jpg|left|200px]] |
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| - | '''Structure of glutathione amide reductase from Chromatium gracile in complex with NAD''' | + | {{Structure |
| + | |PDB= 2rab |SIZE=350|CAPTION= <scene name='initialview01'>2rab</scene>, resolution 2.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+464'>AC1</scene>, <scene name='pdbsite=AC2:Ni+Binding+Site+For+Residue+A+466'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+B+464'>AC3</scene>, <scene name='pdbsite=AC4:Ni+Binding+Site+For+Residue+B+466'>AC4</scene>, <scene name='pdbsite=AC5:Ni+Binding+Site+For+Residue+A+468'>AC5</scene>, <scene name='pdbsite=AC6:Ni+Binding+Site+For+Residue+B+468'>AC6</scene>, <scene name='pdbsite=AC7:Fad+Binding+Site+For+Residue+A+500'>AC7</scene>, <scene name='pdbsite=AC8:Nad+Binding+Site+For+Residue+A+600'>AC8</scene>, <scene name='pdbsite=AC9:Fad+Binding+Site+For+Residue+B+500'>AC9</scene> and <scene name='pdbsite=BC1:Nad+Binding+Site+For+Residue+B+600'>BC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of glutathione amide reductase from Chromatium gracile in complex with NAD''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2RAB is a [ | + | 2RAB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Marichromatium_gracile Marichromatium gracile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RAB OCA]. |
==Reference== | ==Reference== | ||
| - | Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase., Van Petegem F, De Vos D, Savvides S, Vergauwen B, Van Beeumen J, J Mol Biol. 2007 Dec 7;374(4):883-9. Epub 2007 Sep 29. PMID:[http:// | + | Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase., Van Petegem F, De Vos D, Savvides S, Vergauwen B, Van Beeumen J, J Mol Biol. 2007 Dec 7;374(4):883-9. Epub 2007 Sep 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17977556 17977556] |
[[Category: Marichromatium gracile]] | [[Category: Marichromatium gracile]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: substrate analog]] | [[Category: substrate analog]] | ||
| - | ''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 18:34:04 2008'' |
Revision as of 16:34, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of glutathione amide reductase from Chromatium gracile in complex with NAD
Overview
Glutathione reductase (GR) plays a vital role in maintaining the antioxidant levels of the cytoplasm by catalyzing the reduction of glutathione disulfide to reduced glutathione, thereby using NADPH and flavin adenine dinucleotide as cofactors. Chromatiaceae have evolved an unusual homolog that prefers both a modified substrate (glutathione amide disulfide [GASSAG]) and a different cofactor (NADH). Herein, we present the crystal structure of the Chromatium gracile glutathione amide reductase (GAR) both alone and in complex with NAD(+). An altered charge distribution in the GASSAG binding pocket explains the difference in substrate specificity. The NADH binding pocket of GAR differs from that of wild-type GR as well as that of a low active GR that was engineered to mimic NADH binding. Based on the GAR structure, we propose two attractive rationales for producing an efficient GR enzyme with NADH specificity.
About this Structure
2RAB is a Single protein structure of sequence from Marichromatium gracile. Full crystallographic information is available from OCA.
Reference
Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase., Van Petegem F, De Vos D, Savvides S, Vergauwen B, Van Beeumen J, J Mol Biol. 2007 Dec 7;374(4):883-9. Epub 2007 Sep 29. PMID:17977556
Page seeded by OCA on Thu Mar 20 18:34:04 2008
Categories: Marichromatium gracile | Single protein | Beeumen, J Van. | Petegem, F Van. | Savvides, S. | Vergauwen, B. | Vos, D De. | CL | FAD | NAD | NI | Fad | Glutathione | Nad | Oxidoreductase | Redox | Substrate analog
