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2rab

From Proteopedia

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Structure of glutathione amide reductase from Chromatium gracile in complex with NAD

Structural highlights

2rab is a 2 chain structure with sequence from Marichromatium gracile. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GASHR_MARGR Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vergauwen B, Pauwels F, Jacquemotte F, Meyer TE, Cusanovich MA, Bartsch RG, Van Beeumen JJ. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J Biol Chem. 2001 Jun 15;276(24):20890-7. PMID:11399772 doi:10.1074/jbc.M102026200
↑ Van Petegem F, De Vos D, Savvides S, Vergauwen B, Van Beeumen J. Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase. J Mol Biol. 2007 Dec 7;374(4):883-9. Epub 2007 Sep 29. PMID:17977556 doi:10.1016/j.jmb.2007.09.072

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rab"

@@ Line 3: / Line 3: @@
 <StructureSection load='2rab' size='340' side='right'caption='[[2rab]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chromatium_gracile Chromatium gracile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RAB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RAB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rab]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RAB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r9z|2r9z]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rab OCA], [http://pdbe.org/2rab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rab RCSB], [http://www.ebi.ac.uk/pdbsum/2rab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rab ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rab OCA], [https://pdbe.org/2rab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rab RCSB], [https://www.ebi.ac.uk/pdbsum/2rab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rab ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GASHR_MARGR GASHR_MARGR] Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation.<ref>PMID:11399772</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Chromatium gracile]]
 [[Category: Large Structures]]
-[[Category: Beeumen, J Van]]
+[[Category: Marichromatium gracile]]
-[[Category: Petegem, F Van]]
+[[Category: De Vos D]]
-[[Category: Savvides, S]]
+[[Category: Savvides S]]
-[[Category: Vergauwen, B]]
+[[Category: Van Beeumen J]]
-[[Category: Vos, D De]]
+[[Category: Van Petegem F]]
-[[Category: Fad]]
+[[Category: Vergauwen B]]
-[[Category: Glutathione]]
-[[Category: Nad]]
-[[Category: Oxidoreductase]]
-[[Category: Redox]]
-[[Category: Substrate analog]]

2rab

From Proteopedia

Current revision

Structure of glutathione amide reductase from Chromatium gracile in complex with NAD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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