6mos

Structure of thioredoxin 1 from the thermophilic eubacterium Thermosipho africanus TCF52B

spinqualitylabelsall models 6mos, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mos is a 1 chain structure with sequence from Thermosipho africanus TCF52B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8001373Å Ligands: TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7IEN1_THEAB Publication Abstract from PubMed The thioredoxin system is a ubiquitous oxidoreductase system that consists of the enzyme thioredoxin reductase (TrxR), its cofactor nicotinamide adenine dinucleotide phosphate (NAD(P)H) and the protein thioredoxin (Trx). The system has been comprehensively studied from many organisms, such as Escherichia coli (E. coli); however, structural and functional analysis of this system from thermophilic bacteria has not been as extensive. In this study, Thermosipho africanus, a thermophilic eubacterium, Trx1 (TaTrx1) was successfully cloned, overexpressed and purified, to greater than 95% purity. Inspection of the amino acid sequence of TaTrx1 categorized the protein as a putative Trx. Its ability to reduce the interchain disulfides of insulin, in the presence of dithiothreitol, provided further evidence to suggest that it was a Trx. The three dimensional structure of the protein, determined using X-ray crystallography, provided additional evidence for this. The crystal structure was solved in space group P212121 to 1.8 A resolution and showed the characteristic thioredoxin fold; four beta-strands surrounded by three alpha-helices. The active site of TaTrx1 contained two cysteines that formed a disulfide bridge, and was structurally similar to the active site of EcTrx1. Further studies indicated that TaTrx1 was far more stable than Trx1 of E. coli (EcTrx1). The protein could withstand both higher temperatures and higher concentrations of guanidine hydrochloride before denaturing. Our studies have therefore identified a novel thermophilic putative Trx that structurally and functionally behaves like a Trx. Structure and function of the putative thioredoxin 1 from the thermophilic eubacterium Thermosipho africanus strain TCF52B.,Sahtout N, Kuttiyatveetil JRA, Sanders DAR Biochim Biophys Acta Proteins Proteom. 2019 Apr;1867(4):426-433. doi:, 10.1016/j.bbapap.2019.01.011. Epub 2019 Feb 1. PMID:30716506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA