An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.
Identifieur interne : 000733 ( Main/Corpus ); précédent : 000732; suivant : 000734An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.
Auteurs : Lars Br Utigam ; Catrine Johansson ; Bastian Kubsch ; Michael A. Mcdonough ; Eckhard Bill ; Arne Holmgren ; Carsten BerndtSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Animals (MeSH), Catalytic Domain (MeSH), Cysteine (chemistry), Enzyme Activation (MeSH), Glutaredoxins (chemistry), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Ligands (MeSH), Molecular Sequence Data (MeSH), Protein Binding (MeSH), Protein Multimerization (MeSH), Sequence Homology, Amino Acid (MeSH), Zebrafish (metabolism), Zebrafish Proteins (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Glutaredoxins, Iron-Sulfur Proteins, Zebrafish Proteins.
- metabolism : Zebrafish.
- Amino Acid Motifs, Animals, Catalytic Domain, Enzyme Activation, Humans, Ligands, Molecular Sequence Data, Protein Binding, Protein Multimerization, Sequence Homology, Amino Acid.
Abstract
Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins.
DOI: 10.1016/j.bbrc.2013.05.132
PubMed: 23756812
Links to Exploration step
pubmed:23756812Le document en format XML
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<affiliation><nlm:affiliation>Division for Biochemistry, Department for Medical Biochemistry and Biophysics, Karolinska Institutet, 17177 Stockholm, Sweden.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name>
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<author><name sortKey="Kubsch, Bastian" sort="Kubsch, Bastian" uniqKey="Kubsch B" first="Bastian" last="Kubsch">Bastian Kubsch</name>
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<author><name sortKey="Mcdonough, Michael A" sort="Mcdonough, Michael A" uniqKey="Mcdonough M" first="Michael A" last="Mcdonough">Michael A. Mcdonough</name>
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<author><name sortKey="Bill, Eckhard" sort="Bill, Eckhard" uniqKey="Bill E" first="Eckhard" last="Bill">Eckhard Bill</name>
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<author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.</title>
<author><name sortKey="Br Utigam, Lars" sort="Br Utigam, Lars" uniqKey="Br Utigam L" first="Lars" last="Br Utigam">Lars Br Utigam</name>
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<author><name sortKey="Kubsch, Bastian" sort="Kubsch, Bastian" uniqKey="Kubsch B" first="Bastian" last="Kubsch">Bastian Kubsch</name>
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<author><name sortKey="Mcdonough, Michael A" sort="Mcdonough, Michael A" uniqKey="Mcdonough M" first="Michael A" last="Mcdonough">Michael A. Mcdonough</name>
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<series><title level="j">Biochemical and biophysical research communications</title>
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<term>Catalytic Domain (MeSH)</term>
<term>Cysteine (chemistry)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Humans (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Ligands (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Zebrafish (metabolism)</term>
<term>Zebrafish Proteins (chemistry)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term>
<term>Glutaredoxins</term>
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<term>Catalytic Domain</term>
<term>Enzyme Activation</term>
<term>Humans</term>
<term>Ligands</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins. </div>
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<ArticleTitle>An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.</ArticleTitle>
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<Abstract><AbstractText>Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins. </AbstractText>
<CopyrightInformation>Copyright © 2013 Elsevier Inc. All rights reserved.</CopyrightInformation>
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