1w4v

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Declercq, J.P.]]
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[[Category: Declercq, J P.]]
[[Category: Evrard, C.]]
[[Category: Evrard, C.]]
[[Category: Smeets, A.]]
[[Category: Smeets, A.]]
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[[Category: thioredoxin]]
[[Category: thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:19:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:33 2008''

Revision as of 13:40, 21 February 2008


1w4v, resolution 1.80Å

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STRUCTURE OF THE OXIDISED 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

1W4V is a Single protein structure of sequence from Homo sapiens. Known structural/functional Site: . 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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