1w89
From Proteopedia
(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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| - | [[Image:1w89.gif|left|200px]]<br /> | + | [[Image:1w89.gif|left|200px]]<br /><applet load="1w89" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1w89" size=" | + | |
caption="1w89, resolution 2.00Å" /> | caption="1w89, resolution 2.00Å" /> | ||
'''STRUCTURE OF THE REDUCED FORM OF HUMAN THIOREDOXIN 2'''<br /> | '''STRUCTURE OF THE REDUCED FORM OF HUMAN THIOREDOXIN 2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mammalian thioredoxin 2 is a mitochondrial isoform of highly evolutionary | + | 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== | ||
| - | 1W89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1W89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W89 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Declercq, J | + | [[Category: Declercq, J P.]] |
[[Category: Evrard, C.]] | [[Category: Evrard, C.]] | ||
[[Category: Smeets, A.]] | [[Category: Smeets, A.]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:28 2008'' |
Revision as of 13:41, 21 February 2008
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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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