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Yorodumi- SASDDD3: Human mitochondrial cysteine desulfurase-ISCU-Frataxin (NFS1, ISD... -
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Basic information
| Entry | Database: SASBDB / ID: SASDDD3 |
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Sample | Human mitochondrial cysteine desulfurase-ISCU-Frataxin (NFS1, ISD11 and Acp heterodimer complex)
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| Function / homology | Function and homology informationpositive regulation of lyase activity / iron-sulfur cluster chaperone activity / negative regulation of iron ion import across plasma membrane / molybdopterin cofactor metabolic process / proprioception / Molybdenum cofactor biosynthesis / L-cysteine desulfurase complex / [4Fe-4S] cluster assembly / Mitochondrial iron-sulfur cluster biogenesis / sulfur carrier activity ...positive regulation of lyase activity / iron-sulfur cluster chaperone activity / negative regulation of iron ion import across plasma membrane / molybdopterin cofactor metabolic process / proprioception / Molybdenum cofactor biosynthesis / L-cysteine desulfurase complex / [4Fe-4S] cluster assembly / Mitochondrial iron-sulfur cluster biogenesis / sulfur carrier activity / Complex III assembly / iron chaperone activity / positive regulation of mitochondrial electron transport, NADH to ubiquinone / Maturation of TCA enzymes and regulation of TCA cycle / negative regulation of organ growth / cysteine desulfurase / cysteine desulfurase activity / Mo-molybdopterin cofactor biosynthetic process / mitochondrial respiratory chain complex III assembly / embryo development ending in birth or egg hatching / Mitochondrial protein import / mitochondrial [2Fe-2S] assembly complex / iron-sulfur cluster assembly complex / oxidative phosphorylation / response to iron ion / [2Fe-2S] cluster assembly / heme biosynthetic process / adult walking behavior / negative regulation of multicellular organism growth / organ growth / lipid A biosynthetic process / iron-sulfur cluster assembly / muscle cell cellular homeostasis / lipid biosynthetic process / ferroxidase / negative regulation of release of cytochrome c from mitochondria / acyl binding / acyl carrier activity / protein autoprocessing / ferroxidase activity / iron-sulfur cluster binding / phosphopantetheine binding / ferric iron binding / protein maturation / enzyme activator activity / iron ion transport / ferrous iron binding / 2 iron, 2 sulfur cluster binding / cellular response to hydrogen peroxide / fatty acid biosynthetic process / pyridoxal phosphate binding / Maturation of replicase proteins / molecular adaptor activity / intracellular iron ion homeostasis / nuclear body / mitochondrial matrix / iron ion binding / response to xenobiotic stimulus / lipid binding / centrosome / negative regulation of apoptotic process / structural molecule activity / protein homodimerization activity / mitochondrion / zinc ion binding / nucleoplasm / metal ion binding / nucleus / membrane / cytoplasm / cytosol Similarity search - Function |
| Biological species | Homo sapiens (human)![]() |
Citation | Journal: Structure / Year: 2018Title: Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering. Authors: Kai Cai / Ronnie O Frederick / Hesam Dashti / John L Markley / ![]() Abstract: Cysteine desulfurase plays a central role in mitochondrial iron-sulfur cluster biogenesis by generating sulfur through the conversion of L-cysteine to L-alanine and by serving as the platform for ...Cysteine desulfurase plays a central role in mitochondrial iron-sulfur cluster biogenesis by generating sulfur through the conversion of L-cysteine to L-alanine and by serving as the platform for assembling other components of the biosynthetic machinery, including ISCU, frataxin, and ferredoxin. The human mitochondrial cysteine desulfurase complex consists of two copies each of NFS1, ISD11, and acyl carrier protein. We describe results from chemical crosslinking coupled with tandem mass spectrometry and small-angle X-ray scattering studies that are consistent with a closed NFS1 dimer rather than an open one for both the cysteine desulfurase-ISCU and cysteine desulfurase-ISCU-frataxin complexes. We present a structural model for the cysteine desulfurase-ISCU-frataxin complex derived from chemical crosslinking restraints in conjunction with the recent crystal structure of the cysteine desulfurase-ISCU-zinc complex and distance constraints from nuclear magnetic resonance. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
-Data source
| SASBDB page | SASDDD3 |
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-Related structure data
| Related structure data | C: citing same article ( |
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| Similar structure data |
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External links
| Related items in Molecule of the Month |
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-Models
| Model #1776 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 4.937284 / P-value: 0.000004 Search similar-shape structures of this assembly by Omokage search (details) |
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Sample
Sample | Name: Human mitochondrial cysteine desulfurase-ISCU-Frataxin (NFS1, ISD11 and Acp heterodimer complex) Specimen concentration: 2.00-10.00 / Entity id: 958 / 959 / 960 / 961 / 962 |
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| Buffer | Name: 20 mM HEPES, 150 mM NaCl, 5 mM TCEP / pH: 7.5 / Comment: HNT Buffer |
| Entity #958 | Name: NFS1 / Type: protein / Description: Cysteine desulfurase, mitochondrial / Formula weight: 44.913 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q9Y697 Sequence: GPVLRPLYMD VQATTPLDPR VLDAMLPYLI NYYGNPHSRT HAYGWESEAA MERARQQVAS LIGADPREII FTSGATESNN IAIKGVARFY RSRKKHLITT QTEHKCVLDS CRSLEAEGFQ VTYLPVQKSG IIDLKELEAA IQPDTSLVSV MTVNNEIGVK QPIAEIGRIC ...Sequence: GPVLRPLYMD VQATTPLDPR VLDAMLPYLI NYYGNPHSRT HAYGWESEAA MERARQQVAS LIGADPREII FTSGATESNN IAIKGVARFY RSRKKHLITT QTEHKCVLDS CRSLEAEGFQ VTYLPVQKSG IIDLKELEAA IQPDTSLVSV MTVNNEIGVK QPIAEIGRIC SSRKVYFHTD AAQAVGKIPL DVNDMKIDLM SISGHKIYGP KGVGAIYIRR RPRVRVEALQ SGGGQERGMR SGTVPTPLVV GLGAACEVAQ QEMEYDHKRI SKLSERLIQN IMKSLPDVVM NGDPKHHYPG CINLSFAYVE GESLLMALKD VALSSGSACT SASLEPSYVL RAIGTDEDLA HSSIRFGIGR FTTEEEVDYT VEKCIQHVKR LREMSPLWEM VQDGIDLKSI KWTQH |
| Entity #959 | Name: ISD11 / Type: protein / Description: LYR motif-containing protein 4 / Formula weight: 11.581 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q9HD34 Sequence: MAASSRAQVL SLYRAMLRES KRFSAYNYRT YAVRRIRDAF RENKNVKDPV EIQTLVNKAK RDLGVIRRQV HIGQLYSTDK LIIENRDMPR THHHHHH |
| Entity #960 | Type: protein / Description: Acyl carrier protein / Formula weight: 11.5 / Num. of mol.: 2 / Source: Escherichia coli (strain K12) / References: UniProt: P0A6A8 Sequence: PspP0A6A8A CPECOLIAcy lcarrierpr oteinOSEsc herichiaco li(strainK12)GNacpPP E1SV2MSTIE ERVKKIIGEQ LGVKQEEVTN NASFVEDLGA DSLDTVELVM ALEEEFDTEI PDEEAEKITT VQAAIDYING HQA |
| Entity #961 | Name: ISCU / Type: protein Description: Iron-sulfur cluster assembly enzyme ISCU, mitochondrial Formula weight: 14.655 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q9H1K1 Sequence: RLYHKKVVDH YENPRNVGSL DKTSKNVGTG LVGAPACGDV MKLQIQVDEK GKIVDARFKT FGCGSAIASS SLATEWVKGK TVEEALTIKN TDIAKELCLP PVKLHCSMLA EDAIKAALAD YKLKQEPKKG EAEKK |
| Entity #962 | Name: FXN / Type: protein / Description: Frataxin, mitochondrial / Formula weight: 14.268 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q16595 Sequence: SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA |
-Experimental information
| Beam | Instrument name: NMRFAM Bruker Nanostar / City: Madison, WI / 国: USA / Type of source: X-ray in house / Wavelength: 0.15418 Å / Dist. spec. to detc.: 1 mm | ||||||||||||||||||||||||||||||||||||
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| Detector | Name: VÅNTEC-2000 / Type: MikroGap / Pixsize x: 200 mm | ||||||||||||||||||||||||||||||||||||
| Scan | Measurement date: Apr 18, 2017 / Storage temperature: 25 °C / Cell temperature: 25 °C / Exposure time: 3600 sec. / Number of frames: 4 / Unit: 1/A /
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| Distance distribution function P(R) |
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| Result | Comments: The solution SAXS study of cysteine desulfurase complex containing ISCU and Frataxin
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