1h6v
From Proteopedia
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[[Category: pyridine nucleotide-disulfide oxidoreductase]] | [[Category: pyridine nucleotide-disulfide oxidoreductase]] | ||
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Revision as of 13:25, 30 October 2007
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MAMMALIAN THIOREDOXIN REDUCTASE
Overview
Thioredoxin reductases (TrxRs) from mammalian cells contain an essential, selenocysteine residue in the conserved C-terminal sequence, Gly-Cys-SeCys-Gly forming a selenenylsulfide in the oxidized enzyme., Reduction by NADPH generates a selenolthiol, which is the active site in, reduction of Trx. The three-dimensional structure of the SeCys498Cys, mutant of rat TrxR in complex with NADP(+) has been determined to 3.0-A, resolution by x-ray crystallography. The overall structure is similar to, that of glutathione reductase (GR), including conserved amino acid, residues binding the cofactors FAD and NADPH. Surprisingly, all residues, directly interacting with the substrate glutathione disulfide in GR are, conserved despite the failure of glutathione disulfide to act as a, substrate for TrxR. ... [(full description)]
About this Structure
1H6V is a [Single protein] structure of sequence from [Rattus norvegicus] with FAD and NDP as [ligands]. Active as [Transferred entry: 1.8.1.9], with EC number [1.6.4.5]. Structure known Active Sites: FAA, FAB, FAC, FAD, FAE, FAF, NDA, NDB, NDC, NDD, NDE and NDF. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme., Sandalova T, Zhong L, Lindqvist Y, Holmgren A, Schneider G, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9533-8. Epub 2001 Jul 31. PMID:11481439
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