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- SASDAY6: IcsS-dimer and IscU-dimer complex (Cysteine desulfurase IscS + Ir... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDAY6 |
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![]() | IcsS-dimer and IscU-dimer complex
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Function / homology | ![]() IscS-TusA complex / oxazole or thiazole biosynthetic process / tRNA 4-thiouridine biosynthesis / IscS-IscU complex / sulfur compound transport / selenocysteine catabolic process / sulfurtransferase complex / sulfur carrier activity / detection of UV / selenocysteine lyase activity ...IscS-TusA complex / oxazole or thiazole biosynthetic process / tRNA 4-thiouridine biosynthesis / IscS-IscU complex / sulfur compound transport / selenocysteine catabolic process / sulfurtransferase complex / sulfur carrier activity / detection of UV / selenocysteine lyase activity / tRNA wobble position uridine thiolation / L-cysteine desulfurase complex / cysteine desulfurase / cysteine desulfurase activity / L-cysteine catabolic process / thiamine biosynthetic process / [2Fe-2S] cluster assembly / iron-sulfur cluster assembly / ferrous iron binding / 2 iron, 2 sulfur cluster binding / pyridoxal phosphate binding / 4 iron, 4 sulfur cluster binding / intracellular iron ion homeostasis / copper ion binding / zinc ion binding / identical protein binding / metal ion binding / cytosol / cytoplasm Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() Title: Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Authors: Filippo Prischi / Petr V Konarev / Clara Iannuzzi / Chiara Pastore / Salvatore Adinolfi / Stephen R Martin / Dmitri I Svergun / Annalisa Pastore / ![]() Abstract: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin ...Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin to iron-sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Models
Model #227 | ![]() Type: dummy / Software: DAMMIF / Radius of dummy atoms: 4.30 A / Symmetry: P2 / Chi-square value: 1.471369 ![]() |
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Model #228 | ![]() Type: atomic / Software: SASREF / Radius of dummy atoms: 1.90 A / Symmetry: P2 / Chi-square value: 2.262016 ![]() |
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Sample
![]() | Name: IcsS-dimer and IscU-dimer complex / Specimen concentration: 5 mg/ml / Entity id: 135 / 138 |
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Buffer | Name: Tris-HCl / Concentration: 20.00 mM / pH: 8 / Composition: 150 mM NaCl and 10 mM β-mercaptoethanol |
Entity #135 | Type: protein / Description: Cysteine desulfurase IscS / Formula weight: 43.597 / Num. of mol.: 2 / Source: Escherichia coli / References: UniProt: P0A6B7 Sequence: KLPIYLDYSA TTPVDPRVAE KMMQFMTMDG TFGNPASRSH RFGWQAEEAV DIARNQIADL VGADPREIVF TSGATESDNL AIKGAANFYQ KKGKHIITSK TEHKAVLDTC RQLEREGFEV TYLAPQRNGI IDLKELEAAM RDDTILVSIM HVNNEIGVVQ DIAAIGEMCR ...Sequence: KLPIYLDYSA TTPVDPRVAE KMMQFMTMDG TFGNPASRSH RFGWQAEEAV DIARNQIADL VGADPREIVF TSGATESDNL AIKGAANFYQ KKGKHIITSK TEHKAVLDTC RQLEREGFEV TYLAPQRNGI IDLKELEAAM RDDTILVSIM HVNNEIGVVQ DIAAIGEMCR ARGIIYHVDA TQSVGKLPID LSQLKVDLMS FSGHKIYGPK GIGALYVRRK PRVRIEAQMH GGGHERGMRS GTLPVHQIVG MGEAYRIAKE EMATEMERLR GLRNRLWNGI KDIEEVYLNG DLEHGAPNIL NVSFNYVEGE SLIMALKDLA VSSGSACTSA SLEPSYVLRA LGLNDELAHS SIRFSLGRFT TEEEIDYTIE LVRKSIGRLR DLSPLWEMYK Q |
Entity #138 | Type: protein Description: Iron-sulfur cluster assembly scaffold protein IscU Formula weight: 14.464 / Num. of mol.: 2 / Source: Escherichia coli / References: UniProt: P0ACD4 Sequence: MAYSEKVIDH YENPRNVGSL DKKDSNVGTG MVGAPACGDV MQLQIKVDDN GIIEDAKFKT YGCGSAIASS SLITEWVKGK SLEEAGAIKN SQIAEELELP PVKVHCSILA EDAIKAAIAD YKAKQGLEHH HHHH |
-Experimental information
Beam | Instrument name: ![]() ![]() ![]() | ||||||||||||||||||
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Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||
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Distance distribution function P(R) |
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Result | Comments: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have ...Comments: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have linked frataxin to iron–sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions.
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