2RAB

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

Summary for 2RAB

• Entry DOI: 10.2210/pdb2rab/pdb
• Related: 2R9Z
• Descriptor: glutathione amide reductase, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: glutathione, substrate analog, nad, fad, redox, oxidoreductase
• Biological source: Marichromatium gracile
• Total number of polymer chains: 2
• Total formula weight: 101839.64

Authors

Van Petegem, F.,De Vos, D.,Savvides, S.,Vergauwen, B.,Van Beeumen, J. (deposition date: 2007-09-14, release date: 2008-02-19, Last modification date: 2024-10-30)

Primary citation

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., 374:883-889, 2007

PubMed Abstract: 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.

PubMed: 17977556
DOI: 10.1016/j.jmb.2007.09.072

Experimental method

X-RAY DIFFRACTION (2.5 Å)