Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.
Identifieur interne : 003800 ( Main/Exploration ); précédent : 003799; suivant : 003801Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.
Auteurs : Johannes Melchers [Allemagne] ; Michael Diechtierow ; Krisztina Fehér ; Irmgard Sinning ; Ivo Tews ; R Luise Krauth-Siegel ; Claudia Muhle-GollSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Analyse de mutations d'ADN (MeSH), Animaux (MeSH), Conformation des protéines (MeSH), Cystéine (composition chimique), Données de séquences moléculaires (MeSH), Liaison aux protéines (MeSH), Lysine (composition chimique), Modèles biologiques (MeSH), Oxygène (composition chimique), Peroxidases (composition chimique), Protéines de protozoaire (composition chimique), Similitude de séquences d'acides aminés (MeSH), Spectroscopie par résonance magnétique (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Trypanosoma brucei brucei (MeSH).
- MESH :
- composition chimique : Cystéine, Lysine, Oxygène, Peroxidases, Protéines de protozoaire, Thiorédoxines.
- Analyse de mutations d'ADN, Animaux, Conformation des protéines, Données de séquences moléculaires, Liaison aux protéines, Modèles biologiques, Similitude de séquences d'acides aminés, Spectroscopie par résonance magnétique, Séquence d'acides aminés, Trypanosoma brucei brucei.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cysteine (chemistry), DNA Mutational Analysis (MeSH), Lysine (chemistry), Magnetic Resonance Spectroscopy (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Oxygen (chemistry), Peroxidases (chemistry), Protein Binding (MeSH), Protein Conformation (MeSH), Protozoan Proteins (chemistry), Sequence Homology, Amino Acid (MeSH), Thioredoxins (chemistry), Trypanosoma brucei brucei (MeSH).
- MESH :
- chemical , chemistry : Cysteine, Lysine, Oxygen, Peroxidases, Protozoan Proteins, Thioredoxins.
- Amino Acid Sequence, Animals, DNA Mutational Analysis, Magnetic Resonance Spectroscopy, Models, Biological, Molecular Sequence Data, Protein Binding, Protein Conformation, Sequence Homology, Amino Acid, Trypanosoma brucei brucei.
Abstract
Trypanosoma brucei, the causative agent of African sleeping sickness, encodes three cysteine homologues (Px I-III) of classical selenocysteine-containing glutathione peroxidases. The enzymes obtain their reducing equivalents from the unique trypanothione (bis(glutathionyl)spermidine)/tryparedoxin system. During catalysis, these tryparedoxin peroxidases cycle between an oxidized form with an intramolecular disulfide bond between Cys(47) and Cys(95) and the reduced peroxidase with both residues in the thiol state. Here we report on the three-dimensional structures of oxidized T. brucei Px III at 1.4A resolution obtained by x-ray crystallography and of both the oxidized and the reduced protein determined by NMR spectroscopy. Px III is a monomeric protein unlike the homologous poplar thioredoxin peroxidase (TxP). The structures of oxidized and reduced Px III are essentially identical in contrast to what was recently found for TxP. In Px III, Cys(47), Gln(82), and Trp(137) do not form the catalytic triad observed in the selenoenzymes, and related proteins and the latter two residues are unaffected by the redox state of the protein. The mutational analysis of three conserved lysine residues in the vicinity of the catalytic cysteines revealed that exchange of Lys(107) against glutamate abrogates the reduction of hydrogen peroxide, whereas Lys(97) and Lys(99) play a crucial role in the interaction with tryparedoxin.
DOI: 10.1074/jbc.M803563200
PubMed: 18684708
PubMed Central: PMC2662087
Affiliations:
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résonance magnétique</term><term>Séquence d'acides aminés</term><term>Trypanosoma brucei brucei</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Trypanosoma brucei, the causative agent of African sleeping sickness, encodes three cysteine homologues (Px I-III) of classical selenocysteine-containing glutathione peroxidases. The enzymes obtain their reducing equivalents from the unique trypanothione (bis(glutathionyl)spermidine)/tryparedoxin system. During catalysis, these tryparedoxin peroxidases cycle between an oxidized form with an intramolecular disulfide bond between Cys(47) and Cys(95) and the reduced peroxidase with both residues in the thiol state. Here we report on the three-dimensional structures of oxidized T. brucei Px III at 1.4A resolution obtained by x-ray crystallography and of both the oxidized and the reduced protein determined by NMR spectroscopy. Px III is a monomeric protein unlike the homologous poplar thioredoxin peroxidase (TxP). The structures of oxidized and reduced Px III are essentially identical in contrast to what was recently found for TxP. In Px III, Cys(47), Gln(82), and Trp(137) do not form the catalytic triad observed in the selenoenzymes, and related proteins and the latter two residues are unaffected by the redox state of the protein. The mutational analysis of three conserved lysine residues in the vicinity of the catalytic cysteines revealed that exchange of Lys(107) against glutamate abrogates the reduction of hydrogen peroxide, whereas Lys(97) and Lys(99) play a crucial role in the interaction with tryparedoxin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18684708</PMID><DateCompleted><Year>2008</Year><Month>12</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>44</Issue><PubDate><Year>2008</Year><Month>Oct</Month><Day>31</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.</ArticleTitle><Pagination><MedlinePgn>30401-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M803563200</ELocationID><Abstract><AbstractText>Trypanosoma brucei, the causative agent of African sleeping sickness, encodes three cysteine homologues (Px I-III) of classical selenocysteine-containing glutathione peroxidases. The enzymes obtain their reducing equivalents from the unique trypanothione (bis(glutathionyl)spermidine)/tryparedoxin system. During catalysis, these tryparedoxin peroxidases cycle between an oxidized form with an intramolecular disulfide bond between Cys(47) and Cys(95) and the reduced peroxidase with both residues in the thiol state. Here we report on the three-dimensional structures of oxidized T. brucei Px III at 1.4A resolution obtained by x-ray crystallography and of both the oxidized and the reduced protein determined by NMR spectroscopy. Px III is a monomeric protein unlike the homologous poplar thioredoxin peroxidase (TxP). The structures of oxidized and reduced Px III are essentially identical in contrast to what was recently found for TxP. In Px III, Cys(47), Gln(82), and Trp(137) do not form the catalytic triad observed in the selenoenzymes, and related proteins and the latter two residues are unaffected by the redox state of the protein. The mutational analysis of three conserved lysine residues in the vicinity of the catalytic cysteines revealed that exchange of Lys(107) against glutamate abrogates the reduction of hydrogen peroxide, whereas Lys(97) and Lys(99) play a crucial role in the interaction with tryparedoxin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Melchers</LastName><ForeName>Johannes</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Structure and Biocomputing, EMBL, 69117 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Diechtierow</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fehér</LastName><ForeName>Krisztina</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sinning</LastName><ForeName>Irmgard</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Tews</LastName><ForeName>Ivo</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R Luise</ForeName><Initials>RL</Initials></Author><Author ValidYN="Y"><LastName>Muhle-Goll</LastName><ForeName>Claudia</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2RM5</AccessionNumber><AccessionNumber>2RM6</AccessionNumber><AccessionNumber>3DWV</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>08</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol 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Michael" sort="Diechtierow, Michael" uniqKey="Diechtierow M" first="Michael" last="Diechtierow">Michael Diechtierow</name><name sortKey="Feher, Krisztina" sort="Feher, Krisztina" uniqKey="Feher K" first="Krisztina" last="Fehér">Krisztina Fehér</name><name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name><name sortKey="Muhle Goll, Claudia" sort="Muhle Goll, Claudia" uniqKey="Muhle Goll C" first="Claudia" last="Muhle-Goll">Claudia Muhle-Goll</name><name sortKey="Sinning, Irmgard" sort="Sinning, Irmgard" uniqKey="Sinning I" first="Irmgard" last="Sinning">Irmgard Sinning</name><name sortKey="Tews, Ivo" sort="Tews, Ivo" uniqKey="Tews I" first="Ivo" last="Tews">Ivo Tews</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Melchers, Johannes" sort="Melchers, Johannes" uniqKey="Melchers J" first="Johannes" last="Melchers">Johannes 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