1w89
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(New page: 200px<br /> <applet load="1w89" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w89, resolution 2.00Å" /> '''STRUCTURE OF THE RE...)
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Revision as of 17:41, 12 November 2007
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STRUCTURE OF THE REDUCED FORM OF HUMAN THIOREDOXIN 2
Overview
Mammalian thioredoxin 2 is a mitochondrial isoform of highly evolutionary, conserved thioredoxins. Thioredoxins are small ubiquitous, protein-disulfide oxidoreductases implicated in a large variety of, biological functions. In mammals, thioredoxin 2 is encoded by a nuclear, gene and is targeted to mitochondria by a N-terminal mitochondrial, presequence. Recently, mitochondrial thioredoxin 2 was shown to interact, with components of the mitochondrial respiratory chain and to play a role, in the control of mitochondrial membrane potential, regulating, mitochondrial apoptosis signaling pathway. Here we report the first, crystal structures of a mammalian mitochondrial thioredoxin 2. Crystal, forms of reduced and oxidized human thioredoxin 2 are described at 2.0 and, 1.8 A resolution. Though the folding is rather similar to that of human, cytosolic/nuclear thioredoxin 1, important differences are observed during, the transition between the oxidized and the reduced states of human, thioredoxin 2, compared with human thioredoxin 1. In spite of the absence, of the Cys residue implicated in dimer formation in human thioredoxin 1, dimerization still occurs in the crystal structure of human thioredoxin 2, mainly mediated by hydrophobic contacts, and the dimers are associated to, form two-dimensional polymers. Interestingly, the structure of human, thioredoxin 2 reveals possible interaction domains with human, peroxiredoxin 5, a substrate protein of human thioredoxin 2 in, mitochondria.
About this Structure
1W89 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2., Smeets A, Evrard C, Landtmeters M, Marchand C, Knoops B, Declercq JP, Protein Sci. 2005 Oct;14(10):2610-21. PMID:16195549
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