GlutaredoxinV1, Main, Exploration, bibRecord, 000679

Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.

Identifieur interne : 000679 ( Main/Exploration ); précédent : 000678; suivant : 000680

Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.

Auteurs : Manickam Yogavel [Inde] ; Timir Tripathi [Inde] ; Ankita Gupta [Inde] ; Mudassir Meraj Banday [Inde] ; Stefan Rahlfs [Allemagne] ; Katja Becker [Allemagne] ; Hassan Belrhali [France] ; Amit Sharma [Inde]

Source :

Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2014.

RBID : pubmed:24419382

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Catalytic Domain (MeSH), Crystallography, X-Ray (MeSH), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Plasmodium falciparum (chemistry), Plasmodium falciparum (enzymology), Plasmodium falciparum (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Sequence Alignment (MeSH), Sulfhydryl Compounds (chemistry).
MESH :
- chemical , chemistry : Glutaredoxins, Sulfhydryl Compounds.
- chemical , metabolism : Glutaredoxins, Glutathione.
- chemistry : Plasmodium falciparum.
- enzymology : Plasmodium falciparum.
- metabolism : Plasmodium falciparum.
- Amino Acid Sequence, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Sequence Alignment.

Abstract

Glutaredoxins (Grxs) are redox proteins that use glutathione ((γ)Glu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys. Here, the crystal structure of PfGrx1 has been determined by the sulfur single-wavelength anomalous diffraction (S-SAD) method utilizing intrinsic protein and solvent S atoms. Several residues were modelled with alternate conformations, and an alternate position was refined for the active-site Cys29 owing to radiation damage. The GSH-binding site is occupied by water polygons and buffer molecules. Structural comparison of PfGrx1 with other Grxs and Grx-like proteins revealed that the GSH-binding motifs (CXXC/CXXS, TVP, CDD, Lys26 and Gln/Arg63) are structurally conserved. Both the monothiol and dithiol Grxs possess three conserved water molecules; two of these were located in the GSH-binding site. PfGrx1 has several polar and charged amino-acid substitutions that provide structurally important additional hydrogen bonds and salt bridges missing in other Grxs.

DOI: 10.1107/S1399004713025285
PubMed: 24419382

Affiliations:

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

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plasmodium falciparum (chemistry)</term>
<term>Plasmodium falciparum (enzymology)</term>
<term>Plasmodium falciparum (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sulfhydryl Compounds (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Plasmodium falciparum (composition chimique)</term>
<term>Plasmodium falciparum (enzymologie)</term>
<term>Plasmodium falciparum (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thiols (composition chimique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Sulfhydryl Compounds</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Plasmodium falciparum</term>
<term>Thiols</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Plasmodium falciparum</term>
</keywords>
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<term>Binding Sites</term>
<term>Catalytic Domain</term>
<term>Crystallography, X-Ray</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Sequence Alignment</term>
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<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Sites de fixation</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are redox proteins that use glutathione ((γ)Glu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys. Here, the crystal structure of PfGrx1 has been determined by the sulfur single-wavelength anomalous diffraction (S-SAD) method utilizing intrinsic protein and solvent S atoms. Several residues were modelled with alternate conformations, and an alternate position was refined for the active-site Cys29 owing to radiation damage. The GSH-binding site is occupied by water polygons and buffer molecules. Structural comparison of PfGrx1 with other Grxs and Grx-like proteins revealed that the GSH-binding motifs (CXXC/CXXS, TVP, CDD, Lys26 and Gln/Arg63) are structurally conserved. Both the monothiol and dithiol Grxs possess three conserved water molecules; two of these were located in the GSH-binding site. PfGrx1 has several polar and charged amino-acid substitutions that provide structurally important additional hydrogen bonds and salt bridges missing in other Grxs.</div>
</front>
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<Month>09</Month>
<Day>03</Day>
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<Month>01</Month>
<Day>14</Day>
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<Title>Acta crystallographica. Section D, Biological crystallography</Title>
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<ArticleTitle>Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.</ArticleTitle>
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<Abstract><AbstractText>Glutaredoxins (Grxs) are redox proteins that use glutathione ((γ)Glu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys. Here, the crystal structure of PfGrx1 has been determined by the sulfur single-wavelength anomalous diffraction (S-SAD) method utilizing intrinsic protein and solvent S atoms. Several residues were modelled with alternate conformations, and an alternate position was refined for the active-site Cys29 owing to radiation damage. The GSH-binding site is occupied by water polygons and buffer molecules. Structural comparison of PfGrx1 with other Grxs and Grx-like proteins revealed that the GSH-binding motifs (CXXC/CXXS, TVP, CDD, Lys26 and Gln/Arg63) are structurally conserved. Both the monothiol and dithiol Grxs possess three conserved water molecules; two of these were located in the GSH-binding site. PfGrx1 has several polar and charged amino-acid substitutions that provide structurally important additional hydrogen bonds and salt bridges missing in other Grxs.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yogavel</LastName>
<ForeName>Manickam</ForeName>
<Initials>M</Initials>
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<ForeName>Timir</ForeName>
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<AffiliationInfo><Affiliation>Department of Biochemistry, North-Eastern Hill University, Shillong 792 022, India.</Affiliation>
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<ForeName>Ankita</ForeName>
<Initials>A</Initials>
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</AffiliationInfo>
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<ForeName>Mudassir Meraj</ForeName>
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<ForeName>Stefan</ForeName>
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<ForeName>Katja</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University Giessen, 35392 Giessen, Germany.</Affiliation>
</AffiliationInfo>
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<ForeName>Hassan</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>European Molecular Biology Laboratory, 6 Rue Jules Horowitz, BP 181, 38042 Grenoble, France.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Sharma</LastName>
<ForeName>Amit</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Road, New Delhi 110 067, India.</Affiliation>
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<Month>12</Month>
<Day>24</Day>
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<MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA>
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<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
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<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
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</MeshHeading>
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<MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
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<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">S-SAD</Keyword>
<Keyword MajorTopicYN="N">dithiol</Keyword>
<Keyword MajorTopicYN="N">glutaredoxin</Keyword>
<Keyword MajorTopicYN="N">glutathione</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year>
<Month>06</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2013</Year>
<Month>09</Month>
<Day>11</Day>
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<PubMedPubDate PubStatus="entrez"><Year>2014</Year>
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<PubMedPubDate PubStatus="medline"><Year>2014</Year>
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<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">24419382</ArticleId>
<ArticleId IdType="pii">S1399004713025285</ArticleId>
<ArticleId IdType="doi">10.1107/S1399004713025285</ArticleId>
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</pubmed>
<affiliations><list><country><li>Allemagne</li>
<li>France</li>
<li>Inde</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
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<settlement><li>Grenoble</li>
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<tree><country name="Inde"><noRegion><name sortKey="Yogavel, Manickam" sort="Yogavel, Manickam" uniqKey="Yogavel M" first="Manickam" last="Yogavel">Manickam Yogavel</name>
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<name sortKey="Banday, Mudassir Meraj" sort="Banday, Mudassir Meraj" uniqKey="Banday M" first="Mudassir Meraj" last="Banday">Mudassir Meraj Banday</name>
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<name sortKey="Sharma, Amit" sort="Sharma, Amit" uniqKey="Sharma A" first="Amit" last="Sharma">Amit Sharma</name>
<name sortKey="Tripathi, Timir" sort="Tripathi, Timir" uniqKey="Tripathi T" first="Timir" last="Tripathi">Timir Tripathi</name>
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<country name="Allemagne"><noRegion><name sortKey="Rahlfs, Stefan" sort="Rahlfs, Stefan" uniqKey="Rahlfs S" first="Stefan" last="Rahlfs">Stefan Rahlfs</name>
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<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Belrhali, Hassan" sort="Belrhali, Hassan" uniqKey="Belrhali H" first="Hassan" last="Belrhali">Hassan Belrhali</name>
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	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.

Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.

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