GlutaredoxinV1, Main, Exploration, bibRecord, 000A16

Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography.

Identifieur interne : 000A16 ( Main/Exploration ); précédent : 000A15; suivant : 000A17

Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography.

Auteurs : Francesco Angelucci [Italie] ; Daniela Dimastrogiovanni ; Giovanna Boumis ; Maurizio Brunori ; Adriana E. Miele ; Fulvio Saccoccia ; Andrea Bellelli

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2010.

RBID : pubmed:20659890

Descripteurs français

KwdFr :
- Animaux (MeSH), Catalyse (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (métabolisme), Cristallographie aux rayons X (méthodes), Données de séquences moléculaires (MeSH), Humains (MeSH), Modèles moléculaires (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (métabolisme), NADP (métabolisme), Oxydoréduction (MeSH), Schistosoma mansoni (enzymologie), Structure tertiaire des protéines (MeSH), Électrons (MeSH).
MESH :
- composition chimique : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- enzymologie : Schistosoma mansoni.
- métabolisme : Complexes multienzymatiques, NADH, NADPH oxidoreductases, NADP.
- méthodes : Cristallographie aux rayons X.
- Animaux, Catalyse, Données de séquences moléculaires, Humains, Modèles moléculaires, Oxydoréduction, Structure tertiaire des protéines, Électrons.

English descriptors

KwdEn :
- Animals (MeSH), Catalysis (MeSH), Crystallography, X-Ray (methods), Electrons (MeSH), Humans (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Multienzyme Complexes (chemistry), Multienzyme Complexes (metabolism), NADH, NADPH Oxidoreductases (chemistry), NADH, NADPH Oxidoreductases (metabolism), NADP (metabolism), Oxidation-Reduction (MeSH), Protein Structure, Tertiary (MeSH), Schistosoma mansoni (enzymology).
MESH :
- chemical , chemistry : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , metabolism : Multienzyme Complexes, NADH, NADPH Oxidoreductases, NADP.
- enzymology : Schistosoma mansoni.
- methods : Crystallography, X-Ray.
- Animals, Catalysis, Electrons, Humans, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Structure, Tertiary.

Abstract

Schistosomiasis is the second most widespread human parasitic disease. It is principally treated with one drug, praziquantel, that is administered to 100 million people each year; less sensitive strains of schistosomes are emerging. One of the most appealing drug targets against schistosomiasis is thioredoxin glutathione reductase (TGR). This natural chimeric enzyme is a peculiar fusion of a glutaredoxin domain with a thioredoxin selenocysteine (U)-containing reductase domain. Selenocysteine is located on a flexible C-terminal arm that is usually disordered in the available structures of the protein and is essential for the full catalytic activity of TGR. In this study, we dissect the catalytic cycle of Schistosoma mansoni TGR by structural and functional analysis of the U597C mutant. The crystallographic data presented herein include the following: the oxidized form (at 1.9 Å resolution); the NADPH- and GSH-bound forms (2.3 and 1.9 Å, respectively); and a different crystal form of the (partially) reduced enzyme (3.1 Å), showing the physiological dimer and the entire C terminus of one subunit. Whenever possible, we determined the rate constants for the interconversion between the different oxidation states of TGR by kinetic methods. By combining the crystallographic analysis with computer modeling, we were able to throw further light on the mechanism of action of S. mansoni TGR. In particular, we hereby propose the putative functionally relevant conformational change of the C terminus after the transfer of reducing equivalents from NADPH to the redox sites of the enzyme.

DOI: 10.1074/jbc.M110.141960
PubMed: 20659890
PubMed Central: PMC2952258

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000986
to stream Main, to step Curation: 000986

Le document en format XML

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<term>Cristallographie aux rayons X (méthodes)</term>
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<term>Schistosoma mansoni (enzymologie)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Électrons (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Schistosomiasis is the second most widespread human parasitic disease. It is principally treated with one drug, praziquantel, that is administered to 100 million people each year; less sensitive strains of schistosomes are emerging. One of the most appealing drug targets against schistosomiasis is thioredoxin glutathione reductase (TGR). This natural chimeric enzyme is a peculiar fusion of a glutaredoxin domain with a thioredoxin selenocysteine (U)-containing reductase domain. Selenocysteine is located on a flexible C-terminal arm that is usually disordered in the available structures of the protein and is essential for the full catalytic activity of TGR. In this study, we dissect the catalytic cycle of Schistosoma mansoni TGR by structural and functional analysis of the U597C mutant. The crystallographic data presented herein include the following: the oxidized form (at 1.9 Å resolution); the NADPH- and GSH-bound forms (2.3 and 1.9 Å, respectively); and a different crystal form of the (partially) reduced enzyme (3.1 Å), showing the physiological dimer and the entire C terminus of one subunit. Whenever possible, we determined the rate constants for the interconversion between the different oxidation states of TGR by kinetic methods. By combining the crystallographic analysis with computer modeling, we were able to throw further light on the mechanism of action of S. mansoni TGR. In particular, we hereby propose the putative functionally relevant conformational change of the C terminus after the transfer of reducing equivalents from NADPH to the redox sites of the enzyme.</div>
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<Abstract><AbstractText>Schistosomiasis is the second most widespread human parasitic disease. It is principally treated with one drug, praziquantel, that is administered to 100 million people each year; less sensitive strains of schistosomes are emerging. One of the most appealing drug targets against schistosomiasis is thioredoxin glutathione reductase (TGR). This natural chimeric enzyme is a peculiar fusion of a glutaredoxin domain with a thioredoxin selenocysteine (U)-containing reductase domain. Selenocysteine is located on a flexible C-terminal arm that is usually disordered in the available structures of the protein and is essential for the full catalytic activity of TGR. In this study, we dissect the catalytic cycle of Schistosoma mansoni TGR by structural and functional analysis of the U597C mutant. The crystallographic data presented herein include the following: the oxidized form (at 1.9 Å resolution); the NADPH- and GSH-bound forms (2.3 and 1.9 Å, respectively); and a different crystal form of the (partially) reduced enzyme (3.1 Å), showing the physiological dimer and the entire C terminus of one subunit. Whenever possible, we determined the rate constants for the interconversion between the different oxidation states of TGR by kinetic methods. By combining the crystallographic analysis with computer modeling, we were able to throw further light on the mechanism of action of S. mansoni TGR. In particular, we hereby propose the putative functionally relevant conformational change of the C terminus after the transfer of reducing equivalents from NADPH to the redox sites of the enzyme.</AbstractText>
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Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography.

Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography.

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