PoplarV1, Main, Exploration, bibRecord, 004072

Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.

Identifieur interne : 004072 ( Main/Exploration ); précédent : 004071; suivant : 004073

Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.

Auteurs : Aude Echalier [France] ; Xavier Trivelli ; Catherine Corbier ; Nicolas Rouhier ; Olivier Walker ; Pascale Tsan ; Jean-Pierre Jacquot ; André Aubry ; Isabelle Krimm ; Jean-Marc Lancelin

Source :

Biochemistry [ 0006-2960 ] ; 2005.

RBID : pubmed:15697201

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Consensus Sequence (MeSH), Crystallization (MeSH), Crystallography, X-Ray (MeSH), Dimerization (MeSH), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (methods), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Peroxidases (chemistry), Peroxidases (metabolism), Peroxiredoxins (MeSH), Plant Proteins (chemistry), Plant Proteins (metabolism), Populus (enzymology), Solutions (MeSH), Surface Properties (MeSH), Thermodynamics (MeSH), Thioredoxins (chemistry), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Oxidoreductases, Peroxidases, Plant Proteins, Thioredoxins.
- chemical , metabolism : Oxidoreductases, Peroxidases, Plant Proteins, Thioredoxins.
- chemical : Glutaredoxins, Peroxiredoxins, Solutions.
- enzymology : Populus.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Amino Acid Sequence, Binding Sites, Consensus Sequence, Crystallization, Crystallography, X-Ray, Dimerization, Molecular Sequence Data, Surface Properties, Thermodynamics.

Abstract

Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.

DOI: 10.1021/bi048226s
PubMed: 15697201

Affiliations:

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

to stream Main, to step Corpus: 004120
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Le document en format XML

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<term>Binding Sites (MeSH)</term>
<term>Consensus Sequence (MeSH)</term>
<term>Crystallization (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Dimerization (MeSH)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Nuclear Magnetic Resonance, Biomolecular (methods)</term>
<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (metabolism)</term>
<term>Peroxiredoxins (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Solutions (MeSH)</term>
<term>Surface Properties (MeSH)</term>
<term>Thermodynamics (MeSH)</term>
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<term>Thioredoxins (metabolism)</term>
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<term>Cristallographie aux rayons X (MeSH)</term>
<term>Dimérisation (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Peroxidases (composition chimique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxirédoxines (MeSH)</term>
<term>Populus (enzymologie)</term>
<term>Propriétés de surface (MeSH)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Résonance magnétique nucléaire biomoléculaire (méthodes)</term>
<term>Sites de fixation (MeSH)</term>
<term>Solutions (MeSH)</term>
<term>Séquence consensus (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thermodynamique (MeSH)</term>
<term>Thiorédoxines (composition chimique)</term>
<term>Thiorédoxines (métabolisme)</term>
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<term>Thioredoxins</term>
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<term>Solutions</term>
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<term>Thiorédoxines</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Nuclear Magnetic Resonance, Biomolecular</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term>
<term>Peroxidases</term>
<term>Protéines végétales</term>
<term>Thiorédoxines</term>
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<term>Binding Sites</term>
<term>Consensus Sequence</term>
<term>Crystallization</term>
<term>Crystallography, X-Ray</term>
<term>Dimerization</term>
<term>Molecular Sequence Data</term>
<term>Surface Properties</term>
<term>Thermodynamics</term>
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<term>Cristallographie aux rayons X</term>
<term>Dimérisation</term>
<term>Données de séquences moléculaires</term>
<term>Glutarédoxines</term>
<term>Peroxirédoxines</term>
<term>Propriétés de surface</term>
<term>Sites de fixation</term>
<term>Solutions</term>
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<front><div type="abstract" xml:lang="en">Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.</div>
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<Abstract><AbstractText>Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.</AbstractText>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
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   |texte=   Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
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Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.

Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.

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