Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery.
Identifieur interne : 000205 ( Main/Exploration ); précédent : 000204; suivant : 000206Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery.
Auteurs : Veronica Nasta [Italie] ; Stefano Da Vela [Allemagne] ; Spyridon Gourdoupis [Italie] ; Simone Ciofi-Baffoni [Italie] ; Dmitri I. Svergun [Allemagne] ; Lucia Banci [Italie]Source :
- Scientific reports [ 2045-2322 ] ; 2019.
Descripteurs français
- KwdFr :
- Analyse de regroupements (MeSH), Diffraction des rayons X (MeSH), Diffusion aux petits angles (MeSH), Ferrosulfoprotéines (composition chimique), Humains (MeSH), Mitochondries (métabolisme), Modèles moléculaires (MeSH), Multimérisation de protéines (MeSH), Mutation (génétique), Protéines de transport (composition chimique).
- MESH :
- composition chimique : Ferrosulfoprotéines, Protéines de transport.
- génétique : Mutation.
- métabolisme : Mitochondries.
- Analyse de regroupements, Diffraction des rayons X, Diffusion aux petits angles, Humains, Modèles moléculaires, Multimérisation de protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Carrier Proteins, Iron-Sulfur Proteins.
- genetics : Mutation.
- metabolism : Mitochondria.
- Cluster Analysis, Humans, Models, Molecular, Protein Multimerization, Scattering, Small Angle, X-Ray Diffraction.
Abstract
In mitochondria, a complex protein machinery is devoted to the maturation of iron-sulfur cluster proteins. Structural information on the last steps of the machinery, which involve ISCA1, ISCA2 and IBA57 proteins, needs to be acquired in order to define how these proteins cooperate each other. We report here the use of an integrative approach, utilizing information from small-angle X-ray scattering (SAXS) and bioinformatics-driven docking prediction, to determine a low-resolution structural model of the human mitochondrial [2Fe-2S]2+ ISCA2-IBA57 complex. In the applied experimental conditions, all the data converge to a structural organization of dimer of dimers for the [2Fe-2S]2+ ISCA2-IBA57 complex with ISCA2 providing the homodimerization core interface. The [2Fe-2S] cluster is out of the ISCA2 core while being shared with IBA57 in the dimer. The specific interaction pattern identified from the dimeric [2Fe-2S]2+ ISCA2-IBA57 structural model allowed us to define the molecular grounds of the pathogenic Arg146Trp mutation of IBA57. This finding suggests that the dimeric [2Fe-2S] ISCA2-IBA57 hetero-complex is a physiologically relevant species playing a role in mitochondrial [4Fe-4S] protein biogenesis.
DOI: 10.1038/s41598-019-55313-5
PubMed: 31831856
PubMed Central: PMC6908724
Affiliations:
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3, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author><author><name sortKey="Da Vela, Stefano" sort="Da Vela, Stefano" uniqKey="Da Vela S" first="Stefano" last="Da Vela">Stefano Da Vela</name><affiliation wicri:level="3"><nlm:affiliation>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg</wicri:regionArea><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Gourdoupis, Spyridon" 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Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author><author><name sortKey="Svergun, Dmitri I" sort="Svergun, Dmitri I" uniqKey="Svergun D" first="Dmitri I" last="Svergun">Dmitri I. Svergun</name><affiliation wicri:level="3"><nlm:affiliation>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg</wicri:regionArea><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy. banci@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy. banci@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carrier Proteins (chemistry)</term><term>Cluster Analysis (MeSH)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Mitochondria (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Mutation (genetics)</term><term>Protein Multimerization (MeSH)</term><term>Scattering, Small Angle (MeSH)</term><term>X-Ray Diffraction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de regroupements (MeSH)</term><term>Diffraction des rayons X (MeSH)</term><term>Diffusion aux petits angles (MeSH)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Humains (MeSH)</term><term>Mitochondries (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Mutation (génétique)</term><term>Protéines de transport (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mitochondries</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cluster Analysis</term><term>Humans</term><term>Models, Molecular</term><term>Protein Multimerization</term><term>Scattering, Small Angle</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de regroupements</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Humains</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In mitochondria, a complex protein machinery is devoted to the maturation of iron-sulfur cluster proteins. Structural information on the last steps of the machinery, which involve ISCA1, ISCA2 and IBA57 proteins, needs to be acquired in order to define how these proteins cooperate each other. We report here the use of an integrative approach, utilizing information from small-angle X-ray scattering (SAXS) and bioinformatics-driven docking prediction, to determine a low-resolution structural model of the human mitochondrial [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 complex. In the applied experimental conditions, all the data converge to a structural organization of dimer of dimers for the [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 complex with ISCA2 providing the homodimerization core interface. The [2Fe-2S] cluster is out of the ISCA2 core while being shared with IBA57 in the dimer. The specific interaction pattern identified from the dimeric [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 structural model allowed us to define the molecular grounds of the pathogenic Arg146Trp mutation of IBA57. This finding suggests that the dimeric [2Fe-2S] ISCA2-IBA57 hetero-complex is a physiologically relevant species playing a role in mitochondrial [4Fe-4S] protein biogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31831856</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>04</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>12</Month><Day>12</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery.</ArticleTitle><Pagination><MedlinePgn>18986</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-019-55313-5</ELocationID><Abstract><AbstractText>In mitochondria, a complex protein machinery is devoted to the maturation of iron-sulfur cluster proteins. Structural information on the last steps of the machinery, which involve ISCA1, ISCA2 and IBA57 proteins, needs to be acquired in order to define how these proteins cooperate each other. We report here the use of an integrative approach, utilizing information from small-angle X-ray scattering (SAXS) and bioinformatics-driven docking prediction, to determine a low-resolution structural model of the human mitochondrial [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 complex. In the applied experimental conditions, all the data converge to a structural organization of dimer of dimers for the [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 complex with ISCA2 providing the homodimerization core interface. The [2Fe-2S] cluster is out of the ISCA2 core while being shared with IBA57 in the dimer. The specific interaction pattern identified from the dimeric [2Fe-2S]<sup>2+</sup> ISCA2-IBA57 structural model allowed us to define the molecular grounds of the pathogenic Arg146Trp mutation of IBA57. This finding suggests that the dimeric [2Fe-2S] ISCA2-IBA57 hetero-complex is a physiologically relevant species playing a role in mitochondrial [4Fe-4S] protein biogenesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nasta</LastName><ForeName>Veronica</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Da Vela</LastName><ForeName>Stefano</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gourdoupis</LastName><ForeName>Spyridon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciofi-Baffoni</LastName><ForeName>Simone</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Svergun</LastName><ForeName>Dmitri I</ForeName><Initials>DI</Initials><AffiliationInfo><Affiliation>European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, 22607, Hamburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy. banci@cerm.unifi.it.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Florence, Italy. banci@cerm.unifi.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>12</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C585465">IBA57 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000629804">ISCA2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016000" MajorTopicYN="N">Cluster Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053838" MajorTopicYN="N">Scattering, Small Angle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray 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